P20099

PR
Gene name
bisC (b3551, JW5940)
Protein name
Biotin sulfoxide reductase
Names
BDS reductase, BSO reductase, L-methionine-(S)-sulfoxide reductase, Met-S-SO reductase
Species
Escherichia coli (strain K12)
KEGG Pathway
eco:b3551
EC number
1.8.4.13: With a disulfide as acceptor
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

4-106 (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 P20099

Entry ID Method Resolution Chain Position Source
AF-P20099-F1 Predicted AlphaFoldDB

No variants for P20099

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P20099

No associated diseases with P20099

6 regional properties for P20099

Type Name Position InterPro Accession
conserved_site Molybdopterin oxidoreductase, prokaryotic, conserved site 459 - 476 IPR006655-1
conserved_site Molybdopterin oxidoreductase, prokaryotic, conserved site 675 - 702 IPR006655-2
domain Molybdopterin oxidoreductase 56 - 517 IPR006656
domain Molybdopterin dinucleotide-binding domain 636 - 739 IPR006657
domain Molybdopterin oxidoreductase, N-terminal 12 - 52 IPR041460
domain Trimethylamine-N-oxide reductase-like, molybdopterin-binding domain 635 - 760 IPR041954

Functions

Description
EC Number 1.8.4.13 With a disulfide as acceptor
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
outer membrane-bounded periplasmic space The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall.

4 GO annotations of molecular function

Name Definition
electron transfer activity Any molecular entity that serves as an electron acceptor and electron donor in an electron transport chain. An electron transport chain is a process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
L-methionine:thioredoxin-disulfide S-oxidoreductase activity Catalysis of the reaction: L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin.
molybdenum ion binding Binding to a molybdenum ion (Mo).
molybdopterin cofactor binding Binding to a 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.

1 GO annotations of biological process

Name Definition
anaerobic respiration The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which uses compounds other than oxygen (e.g. nitrate, sulfate) as the terminal electron acceptor.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MANSSSRYSV LTAAHWGPML VETDGETVFS SRGALATGME NSLQSAVRDQ VHSNTRVRFP
70 80 90 100 110 120
MVRKGFLASP ENPQGIRGQD EFVRVSWDEA LDLIHQQHKR IREAYGPASI FAGSYGWRSN
130 140 150 160 170 180
GVLHKASTLL QRYMALAGGY TGHLGDYSTG AAQAIMPYVV GGSEVYQQQT SWPLVLEHSD
190 200 210 220 230 240
VVVLWSANPL NTLKIAWNAS DEQGLSYFSA LRDSGKKLIC IDPMRSETVD FFGDKMEWVA
250 260 270 280 290 300
PHMGTDVALM LGIAHTLVEN GWHDEAFLAR CTTGYAVFAS YLLGESDGIA KTAEWAAEIC
310 320 330 340 350 360
GVGAAKIREL AAIFHQNTTM LMAGWGMQRQ QFGEQKHWMI VTLAAMLGQI GTPGGGFGLS
370 380 390 400 410 420
YHFANGGNPT RRSAVLSSMQ GSLPGGCDAV DKIPVARIVE ALENPGGAYQ HNGMNRHFPD
430 440 450 460 470 480
IRFIWWAGGA NFTHHQDTNR LIRAWQKPEL VVISECFWTA AAKHADIVLP ATTSFERNDL
490 500 510 520 530 540
TMTGDYSNQH LVPMKQVVPP RYEARNDFDV FAELSERWEK GGYARFTEGK SELQWLETFY
550 560 570 580 590 600
NVARQRGASQ QVELPPFAEF WQANQLIEMP ENPDSERFIR FADFCRDPLA HPLKTASGKI
610 620 630 640 650 660
EIFSQRIADY GYPDCPGHPM WLEPDEWQGN AEPEQLQVLS AHPAHRLHSQ LNYSSLRELY
670 680 690 700 710 720
AVANREPVTI HPDDAQERGI QDGDTVRLWN ARGQILAGAV ISEGIKPGVI CIHEGAWPDL
730 740 750 760 770
DLTADGICKN GAVNVLTKDL PSSRLGNGCA GNTALAWLEK YNGPELTLTA FEPPASS