Q5R557

PR
Gene name
ALAS2
Protein name
5-aminolevulinate synthase, erythroid-specific, mitochondrial
Names
ALAS-E, 5-aminolevulinic acid synthase 2, Delta-ALA synthase 2, Delta-aminolevulinate synthase 2
Species
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
KEGG Pathway
pon:100174709
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)

71-160 (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 Q5R557

Entry ID Method Resolution Chain Position Source
AF-Q5R557-F1 Predicted AlphaFoldDB

No variants for Q5R557

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5R557

No associated diseases with Q5R557

7 regional properties for Q5R557

Type Name Position InterPro Accession
domain Translational (tr)-type GTP-binding domain 10 - 204 IPR000795
domain Translation elongation factor EFTu/EF1A, C-terminal 298 - 392 IPR004160
domain Translation elongation factor EFTu-like, domain 2 225 - 293 IPR004161
domain Small GTP-binding protein domain 13 - 148 IPR005225
conserved_site Tr-type G domain, conserved site 51 - 66 IPR031157
domain Elongation factor Tu, domain 2 211 - 297 IPR033720
domain Elongation factor Tu (EF-Tu), GTP-binding domain 11 - 203 IPR041709

Functions

Description
EC Number 2.3.1.37 Transferring groups other than amino-acyl groups
Subcellular Localization
  • Mitochondrion inner membrane ; Peripheral membrane protein
  • Localizes to the matrix side of the mitochondrion inner membrane
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
mitochondrial inner membrane The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
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.

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.

2 GO annotations of biological process

Name Definition
protoporphyrinogen IX biosynthetic process The chemical reactions and pathways resulting in the formation of protoporphyrinogen IX.
response to hypoxia Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MVTAAMLLQC CPVPARGPTS LLGKVVKTHQ FLFGIGRCPI LATQGPNCSQ IHLKATKAGG
70 80 90 100 110 120
DSPSWAKGHC PFMLSELQDG KSKIVQKAAP EVQEDVKAFK TDLPSSLVSA SLKKPFSSPQ
130 140 150 160 170 180
EQEQISGKVT HLIQDNMPGN YVFSYDQFFR DKIMEKKQDH TYRVFKTVNR WADAYPFAQH
190 200 210 220 230 240
FSEASVASKD VSVWCSNDYL GMSRHPQVLR ATQETLQRHG AGAGGTRNIS GTSKFHVELE
250 260 270 280 290 300
QELAELHQKD SALLFSSCFV ANDSTLFTLA KILPGCEIYS DAGNHASMIQ GIRNSGAAKF
310 320 330 340 350 360
VFRHNDPDHL KKLLEKSNPK IPKIVAFEAV HSMDGAICPL EELCDVSHQY GALTFVDEVH
370 380 390 400 410 420
AVGLYGSRGA GIGERDGIMH KIDIISGTLG KAFGCVGGYI ASTRDLVDMV RSYAAGFIFT
430 440 450 460 470 480
TSLPPMVLSG ALESVRLLKG EEGQALRRAH QRNVKHMRQL LMDRGLPVIP CPSHIIPIRV
490 500 510 520 530 540
GNAALNSKLC DLLLSKHGIY VQAINYPTVP RGEELLRLAP SPHHSPQMME DFVEKLLLAW
550 560 570 580
TEVGLPLQDV SVAACNFCRR PVHFELMSEW ERSYFGNMGP QYVTTYA