Q75DX7

PR
Gene name
HEM1 (ABL104C)
Protein name
5-aminolevulinate synthase, mitochondrial
Names
5-aminolevulinic acid synthase, Delta-ALA synthase, Delta-aminolevulinate synthase
Species
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
KEGG Pathway
ago:AGOS_ABL104C
EC number
2.3.1.37: Transferring groups other than amino-acyl groups
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

9-105 (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 Q75DX7

Entry ID Method Resolution Chain Position Source
AF-Q75DX7-F1 Predicted AlphaFoldDB

No variants for Q75DX7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q75DX7

No associated diseases with Q75DX7

3 regional properties for Q75DX7

Type Name Position InterPro Accession
binding_site Aminotransferase, class-II, pyridoxal-phosphate binding site 342 - 351 IPR001917
domain Aminotransferase, class I/classII 128 - 487 IPR004839
domain Tetrapyrrole biosynthesis, 5-aminolevulinic acid synthase 85 - 499 IPR010961

Functions

Description
EC Number 2.3.1.37 Transferring groups other than amino-acyl groups
Subcellular Localization
  • Mitochondrion matrix
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

2 GO annotations of molecular function

Name Definition
5-aminolevulinate synthase activity Catalysis of the reaction: glycine + H(+) + succinyl-CoA = 5-aminolevulinate + CO(2) + CoA.
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.

3 GO annotations of biological process

Name Definition
heme biosynthetic process The chemical reactions and pathways resulting in the formation of heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring, from less complex precursors.
positive regulation of organelle assembly Any process that activates or increases the frequency, rate or extent of organelle assembly.
protoporphyrinogen IX biosynthetic process The chemical reactions and pathways resulting in the formation of protoporphyrinogen IX.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MDSLARQSAK ICPFVSRVTS SMQQVQVLHK TNMSAMAQQC PVMRRAMAAR GYVTASPPAG
70 80 90 100 110 120
AAAADVGEAR PITPVLERGT QERTFDYDGL FETELQKKRL DSSYRFFNNI NRLAKEYPMA
130 140 150 160 170 180
HRLEEEDKVT VWCSNDYLTY SRNEKVMETM KRTIDKYGAG AGGTRNIAGH NRHAMRLEAE
190 200 210 220 230 240
LAALHKKEGA LVFSSCFVAN DAVLSLLGQK MPNMVIFSDE MNHASMIMGI KHANVQKHIF
250 260 270 280 290 300
RHNDLQHLEE LLAMYPKSQP KLIAFESVYS MSGSVADIRK ICDLAEKYGA LTFLDEVHSV
310 320 330 340 350 360
GLYGPHGAGV AEHLDFEAHR KAGLASPAQT TVLDRVDMIT ATLGKSFGSV GGYLAASEKL
370 380 390 400 410 420
VDFVRSYAPG FIFTSSLPPA VMAGSAAAVF DQRSSLHLRQ LQQKHTSYVK TGLGDLGIPV
430 440 450 460 470 480
QPNPSHIVPV LVGNPDLAKR ASDILMEKHR IYVQAINFPT VPRGTERLRI TPTPGHTNDL
490 500 510 520 530 540
SDVLLDAMDD VWKTLQLPRV SDWAAHGGLL GVGEPDYVPE ANLWTEEQMS LTNDDLHPSV
550
FSPVEKFLEV SSGIKA