UniProtKB - Q59676 (MUTA_PORGI)
Protein
Methylmalonyl-CoA mutase small subunit
Gene
mutA
Organism
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Status
Functioni
Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates.By similarity
Catalytic activityi
- EC:5.4.99.2
Cofactori
adenosylcob(III)alaminBy similarity
: propanoyl-CoA degradation Pathwayi
This protein is involved in step 3 of the subpathway that synthesizes succinyl-CoA from propanoyl-CoA.Proteins known to be involved in the 3 steps of the subpathway in this organism are:
- no protein annotated in this organism
- no protein annotated in this organism
- Methylmalonyl-CoA mutase small subunit (mutA), Methylmalonyl-CoA mutase large subunit (mutB)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes succinyl-CoA from propanoyl-CoA, the pathway propanoyl-CoA degradation and in Metabolic intermediate metabolism.
GO - Molecular functioni
- cobalamin binding Source: UniProtKB-KW
- metal ion binding Source: InterPro
- methylmalonyl-CoA mutase activity Source: UniProtKB-EC
GO - Biological processi
- lactate fermentation to propionate and acetate Source: InterPro
Keywordsi
Molecular function | Isomerase |
Ligand | Cobalamin, Cobalt |
Enzyme and pathway databases
UniPathwayi | UPA00945;UER00910 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:mutA Synonyms:mcmA Ordered Locus Names:PG_1656 |
Organismi | Porphyromonas gingivalis (strain ATCC BAA-308 / W83) |
Taxonomic identifieri | 242619 [NCBI] |
Taxonomic lineagei | Bacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Porphyromonadaceae › Porphyromonas › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000194267 | 1 – 618 | Methylmalonyl-CoA mutase small subunitAdd BLAST | 618 |
Interactioni
Subunit structurei
Heterodimer of an alpha and a beta chain.
Protein-protein interaction databases
STRINGi | 242619.PG_1656 |
Family & Domainsi
Sequence similaritiesi
Belongs to the methylmalonyl-CoA mutase family.Curated
Phylogenomic databases
eggNOGi | COG1884, Bacteria |
HOGENOMi | CLU_009523_6_0_10 |
OMAi | WYVERLT |
OrthoDBi | 720283at2 |
Family and domain databases
InterProi | View protein in InterPro IPR016176, Cbl-dep_enz_cat IPR036724, Cobalamin-bd_sf IPR006099, MeMalonylCoA_mutase_a/b_cat IPR004608, MMCoA_mutase_b |
Pfami | View protein in Pfam PF01642, MM_CoA_mutase, 1 hit |
SUPFAMi | SSF51703, SSF51703, 1 hit SSF52242, SSF52242, 1 hit |
TIGRFAMsi | TIGR00642, mmCoA_mut_beta, 1 hit |
PROSITEi | View protein in PROSITE PS00544, METMALONYL_COA_MUTASE, 1 hit |
i Sequence
Sequence statusi: Complete.
Q59676-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MAKEKEKLFS EFPPVSREAW IDKITADLKG VPFEKKLVWR TNEGFNVNPF
60 70 80 90 100
YRREDIEDLK TTTSLPDEYP YVRSTRMHNE WLVRQDIVVG DNVAEANEKA
110 120 130 140 150
LDLLNKGVDS LGFYLKKVHI NVDTLAALLK DIELTAVELN FNCCITRAAD
160 170 180 190 200
LLSAFSAYVK KVGADPNKCH GSVSYDPFKK QLVRGVSNPD WVKMTLPVMD
210 220 230 240 250
AARELPAFRV LNVNAVNLSD AGAFITQELG YALAWGAELL DKLTDAGYKP
260 270 280 290 300
EEIASRIKFN FGIGSNYFME IAKFRAARWL WAQIVGSYGD QYKNETAKIH
310 320 330 340 350
QHATTSMWNK TVFDAHVNLL RTQTETMSAA IAGVDSITVL PFDVTYQQSD
360 370 380 390 400
DFSERIARNQ QLLLKEECHF DKVIDPSAGS YYIETLTNSI GEEAWKLFLS
410 420 430 440 450
VEDAGGFTQA AETASIQKAV NASNIKRHQS VATRREIFLG TNQFPNFTEV
460 470 480 490 500
AGDKITLAQG EHDCNCVKSI EPLNFSRGAS EFEALRLATE KSGKTPVVFM
510 520 530 540 550
LTIGNLAMRL ARSQFSSNFF GCAGYKLIDN LGFKSVEEGV DAALAAKADI
560 570 580 590 600
VVLCSSDDEY AEYAPAAFDY LAGRAEFVVA GAPACMADLE AKGIRNYVHV
610
KSNVLETLRA FNDKFGIR
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 332 | A → R in AAB51083 (PubMed:8566763).Curated | 1 | |
Sequence conflicti | 428 – 431 | HQSV → PVG in AAB51083 (PubMed:8566763).Curated | 4 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L30136 Genomic DNA Translation: AAB51083.1 AE015924 Genomic DNA Translation: AAQ66675.1 |
PIRi | JC4559 |
RefSeqi | WP_005875479.1, NC_002950.2 |
Genome annotation databases
EnsemblBacteriai | AAQ66675; AAQ66675; PG_1656 |
GeneIDi | 29255692 |
KEGGi | pgi:PG_1656 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L30136 Genomic DNA Translation: AAB51083.1 AE015924 Genomic DNA Translation: AAQ66675.1 |
PIRi | JC4559 |
RefSeqi | WP_005875479.1, NC_002950.2 |
3D structure databases
SMRi | Q59676 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 242619.PG_1656 |
Genome annotation databases
EnsemblBacteriai | AAQ66675; AAQ66675; PG_1656 |
GeneIDi | 29255692 |
KEGGi | pgi:PG_1656 |
Phylogenomic databases
eggNOGi | COG1884, Bacteria |
HOGENOMi | CLU_009523_6_0_10 |
OMAi | WYVERLT |
OrthoDBi | 720283at2 |
Enzyme and pathway databases
UniPathwayi | UPA00945;UER00910 |
Family and domain databases
InterProi | View protein in InterPro IPR016176, Cbl-dep_enz_cat IPR036724, Cobalamin-bd_sf IPR006099, MeMalonylCoA_mutase_a/b_cat IPR004608, MMCoA_mutase_b |
Pfami | View protein in Pfam PF01642, MM_CoA_mutase, 1 hit |
SUPFAMi | SSF51703, SSF51703, 1 hit SSF52242, SSF52242, 1 hit |
TIGRFAMsi | TIGR00642, mmCoA_mut_beta, 1 hit |
PROSITEi | View protein in PROSITE PS00544, METMALONYL_COA_MUTASE, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | MUTA_PORGI | |
Accessioni | Q59676Primary (citable) accession number: Q59676 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1997 |
Last sequence update: | October 3, 2003 | |
Last modified: | December 2, 2020 | |
This is version 136 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families