B3NY19

PR
Gene name
mal
Protein name
Molybdenum cofactor sulfurase
Names
MCS, MOS, MoCo sulfurase, Molybdenum cofactor sulfurtransferase, Protein maroon-like, Ma-l
Species
Drosophila erecta (Fruit fly)
KEGG Pathway
der:6549751
EC number
2.8.1.9: Sulfurtransferases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

460-534 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for B3NY19

Entry ID Method Resolution Chain Position Source
AF-B3NY19-F1 Predicted AlphaFoldDB

No variants for B3NY19

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B3NY19

No associated diseases with B3NY19

4 regional properties for B3NY19

Type Name Position InterPro Accession
domain Aminotransferase class V domain 29 - 188 IPR000192-1
domain Aminotransferase class V domain 213 - 471 IPR000192-2
domain Molybdenum cofactor sulfurase, C-terminal 619 - 781 IPR005302
domain Molybdenum cofactor sulfurase, middle domain 513 - 631 IPR005303

Functions

Description
EC Number 2.8.1.9 Sulfurtransferases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

5 GO annotations of molecular function

Name Definition
lyase activity Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.
Mo-molybdopterin cofactor sulfurase activity Catalysis of the sulfurylation of the desulfo form of molybdenum cofactor (MoCo), a cofactor required for the activity of some enzymes, such as aldehyde oxidase.
molybdenum cofactor sulfurtransferase activity Catalysis of the reaction: 2 H+ + MoO2-molybdopterin cofactor(2-) + L-cysteine <=> thio-molybdenum cofactor + L-alanine + H2O.
molybdenum ion binding Binding to a molybdenum ion (Mo).
pyridoxal phosphate binding Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.

4 GO annotations of biological process

Name Definition
Mo-molybdopterin cofactor biosynthetic process The chemical reactions and pathways resulting in the formation of the Mo-molybdopterin cofactor, essential for the catalytic activity of some enzymes. The cofactor consists of a mononuclear molybdenum (Mo) ion coordinated by one or two molybdopterin ligands.
molybdopterin cofactor biosynthetic process The chemical reactions and pathways resulting in the formation of the molybdopterin cofactor (Moco), essential for the catalytic activity of some enzymes, e.g. sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. The cofactor consists of a mononuclear molybdenum (Mo-molybdopterin) or tungsten ion (W-molybdopterin) coordinated by one or two molybdopterin ligands.
molybdopterin cofactor metabolic process The chemical reactions and pathways involving the molybdopterin cofactor (Moco), essential for the catalytic activity of some enzymes, e.g. sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. The cofactor consists of a mononuclear molybdenum (Mo-molybdopterin) or tungsten ion (W-molybdopterin) coordinated by one or two molybdopterin ligands.
ommochrome biosynthetic process The chemical reactions and pathways resulting in the formation of ommochromes, any of a large group of natural polycyclic pigments commonly found in the Arthropoda, particularly in the ommatidia of the compound eye.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTPYRPEFSA AEQSRIDAEF SRLARNKTVY LDHAGTTLYA ENQVTAAAEQ LQRNVICNPH
70 80 90 100 110 120
TCRLTGDFVD QVRFKILEFF NTTAEDYHVI FTANATAALS LVAENFDFGS SGDFHFCQEN
130 140 150 160 170 180
HTSVLGMRER VRANGIYMLR EKEISGGGAK ENGTVHQVSG KTGNSLVTFS AQCNFSGYKI
190 200 210 220 230 240
PLDSIEKIQN YGLSKPGKQL WSALGDKKEH THNDYYICLD AASFVATSPL DLRKYRPDYV
250 260 270 280 290 300
CLSFYKIFGY PTGVGALLVS RRGAEVFQKR RFFGGGTINY AFPHAMDYQL RETFHQRYED
310 320 330 340 350 360
GTLPFLSIVG LLEGFRTLER LVPKTDEFST MERISRHVFG LAKYVEDQLR QLQHPNGEPL
370 380 390 400 410 420
VELYNKVGYQ DKARQGGIVA FNVRTESGSF VGFGEIACVA ALHGILLRTG CFCNIGACQY
430 440 450 460 470 480
YLGLDEDALD SIYKRAGRIC GDYFDLVDGQ PTGAVRVSFG YMTTIQDVEQ LLQMLRSSYL
490 500 510 520 530 540
ATKPLQRIQF IEEQAEQLPP LLKERVQLLR PKLLQMAIYP VKSCAAFKIE SPGSWPLTDQ
550 560 570 580 590 600
GLKYDREWMI VDMNGMALTQ KRCTELCLIR PVIKVDQLEL QFGDNSHFSV PLSLEDQAAD
610 620 630 640 650 660
SAKCVSKVCR QPVEGLDCGD AVAQWLSENL GLEGLRLLRQ SGQRNSSKDQ QKLSLVNQAQ
670 680 690 700 710 720
FLLLNRSSVR SLQFEEPLDE TVDRFRANII IDTGSAFEEL TYKALSIGGI QFQVEGPCQR
730 740 750 760 770 780
CDMICINQRT GERSPETLTT ISRLQKGRMR FGIYITRIPP DTKDLEPKEQ HMTCGDVVIV
E