UniProtKB - Q3J4D7 (MCM_RHOS4)
Protein
Methylmalonyl-CoA mutase
Gene
mcm
Organism
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Status
Functioni
Radical enzyme that catalyzes the transformation of (2R)-methylmalonyl-CoA to succinyl-CoA. Is involved in the ethylmalonyl-CoA pathway for acetyl-CoA assimilation required for R.sphaeroides growth on acetate as sole carbon source.1 Publication1 Publication
Catalytic activityi
Cofactori
adenosylcob(III)alamin1 Publication
: propanoyl-CoA degradation Pathwayi
This protein is involved in step 3 of the subpathway that synthesizes succinyl-CoA from propanoyl-CoA.1 PublicationProteins known to be involved in the 3 steps of the subpathway in this organism are:
- Propionyl-CoA carboxylase (pccA), Propionyl-CoA carboxylase beta chain (pccB)
- no protein annotated in this organism
- Methylmalonyl-CoA mutase (mcm)
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.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 195 | SubstrateBy similarity | 1 | |
Binding sitei | 222 | SubstrateBy similarity | 1 | |
Binding sitei | 232 | SubstrateBy similarity | 1 | |
Metal bindingi | 592 | Cobalt (cobalamin axial ligand)By similarity | 1 |
GO - Molecular functioni
- cobalamin binding Source: UniProtKB-KW
- metal ion binding Source: UniProtKB-KW
- methylmalonyl-CoA mutase activity Source: UniProtKB-EC
Keywordsi
Molecular function | Isomerase |
Ligand | Cobalamin, Cobalt, Metal-binding |
Enzyme and pathway databases
BioCyci | MetaCyc:MONOMER-13591 |
UniPathwayi | UPA00945;UER00910 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:mcm2 Publications Synonyms:mcmAImported ORF Names:RSP_2192Imported |
Organismi | Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158) |
Taxonomic identifieri | 272943 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000447589 | 1 – 709 | Methylmalonyl-CoA mutaseAdd BLAST | 709 |
Expressioni
Inductioni
Strongly up-regulated during growth on acetate as sole carbon source.1 Publication
Interactioni
Subunit structurei
Homodimer.
By similarityProtein-protein interaction databases
STRINGi | 272943.RSP_2192 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 579 – 709 | B12-bindingPROSITE-ProRule annotationAdd BLAST | 131 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 73 – 77 | Substrate bindingBy similarity | 5 | |
Regioni | 183 – 185 | Substrate bindingBy similarity | 3 | |
Regioni | 271 – 273 | Substrate bindingBy similarity | 3 |
Sequence similaritiesi
Belongs to the methylmalonyl-CoA mutase family.Curated
Phylogenomic databases
eggNOGi | COG1884, Bacteria COG2185, Bacteria |
OMAi | PTQCGYD |
PhylomeDBi | Q3J4D7 |
Family and domain databases
InterProi | View protein in InterPro IPR006159, Acid_CoA_mut_C IPR016176, Cbl-dep_enz_cat IPR006158, Cobalamin-bd IPR036724, Cobalamin-bd_sf IPR006099, MeMalonylCoA_mutase_a/b_cat IPR006098, MMCoA_mutase_a_cat |
Pfami | View protein in Pfam PF02310, B12-binding, 1 hit PF01642, MM_CoA_mutase, 1 hit |
SUPFAMi | SSF51703, SSF51703, 1 hit SSF52242, SSF52242, 1 hit |
TIGRFAMsi | TIGR00640, acid_CoA_mut_C, 1 hit TIGR00641, acid_CoA_mut_N, 1 hit |
PROSITEi | View protein in PROSITE PS51332, B12_BINDING, 1 hit PS00544, METMALONYL_COA_MUTASE, 1 hit |
i Sequence
Sequence statusi: Complete.
Q3J4D7-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTEDLDAWRK LAEKELKGKS PDSLTWNTLE GIPVKPLYTR ADLAGMEHLD
60 70 80 90 100
GLPGVAPFTR GVRATMYAGR PWTIRQYAGF STAEASNAFY RKALAAGQQG
110 120 130 140 150
VSVAFDLATH RGYDSDHPRV VGDVGKAGVA IDSIEDMKIL FNGIPLEKIS
160 170 180 190 200
VSMTMNGAVI PILANFIVTG EEQGVPRAAL SGTIQNDILK EFMVRNTYIY
210 220 230 240 250
PPEPSMRIIA DIIEYTSKEM PKFNSISISG YHMQEAGANL VQELAYTLAD
260 270 280 290 300
GREYVRAALA RGMNVDDFAG RLSFFFAIGM NFFMEAAKLR AARLLWHRIM
310 320 330 340 350
SEFAPKKPGS LMLRTHCQTS GVSLQEQDPY NNVIRTAYEA MSAALGGTQS
360 370 380 390 400
LHTNALDEAI ALPTEFSARI ARNTQIILQE ETGVTRVVDP LAGSYYVESL
410 420 430 440 450
TAELAEKAWA LIEEVEAMGG MTKAVASGMP KLRIEESAAR RQAAIDRGED
460 470 480 490 500
VIVGVNKYRL AKEDPIEILD IDNVAVRDAQ IARLEKMRAT RDEAACQAAL
510 520 530 540 550
DELTRRAAEG GNLLEAAVDA SRARASVGEI SMAMEKVFGR HRAEVKTLSG
560 570 580 590 600
VYGAAYEGDD GFAQIQRDVE SFAEEEGRRP RMLVVKMGQD GHDRGAKVIA
610 620 630 640 650
TAFADIGFDV DVGTLFQTPE EAAQDAIDND VHVVGISSLA AGHKTLAPKL
660 670 680 690 700
IEALKEKGAG EILVICGGVI PQQDYDFLQQ AGVKAIFGPG TNIPSAAKHI
LDLIREARS
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP000143 Genomic DNA Translation: ABA78347.1 |
RefSeqi | WP_011337301.1, NZ_CP030271.1 YP_352248.1, NC_007493.2 |
Genome annotation databases
EnsemblBacteriai | ABA78347; ABA78347; RSP_2192 |
KEGGi | rsp:RSP_2192 |
PATRICi | fig|272943.9.peg.1091 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP000143 Genomic DNA Translation: ABA78347.1 |
RefSeqi | WP_011337301.1, NZ_CP030271.1 YP_352248.1, NC_007493.2 |
3D structure databases
SMRi | Q3J4D7 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 272943.RSP_2192 |
Genome annotation databases
EnsemblBacteriai | ABA78347; ABA78347; RSP_2192 |
KEGGi | rsp:RSP_2192 |
PATRICi | fig|272943.9.peg.1091 |
Phylogenomic databases
eggNOGi | COG1884, Bacteria COG2185, Bacteria |
OMAi | PTQCGYD |
PhylomeDBi | Q3J4D7 |
Enzyme and pathway databases
UniPathwayi | UPA00945;UER00910 |
BioCyci | MetaCyc:MONOMER-13591 |
Family and domain databases
InterProi | View protein in InterPro IPR006159, Acid_CoA_mut_C IPR016176, Cbl-dep_enz_cat IPR006158, Cobalamin-bd IPR036724, Cobalamin-bd_sf IPR006099, MeMalonylCoA_mutase_a/b_cat IPR006098, MMCoA_mutase_a_cat |
Pfami | View protein in Pfam PF02310, B12-binding, 1 hit PF01642, MM_CoA_mutase, 1 hit |
SUPFAMi | SSF51703, SSF51703, 1 hit SSF52242, SSF52242, 1 hit |
TIGRFAMsi | TIGR00640, acid_CoA_mut_C, 1 hit TIGR00641, acid_CoA_mut_N, 1 hit |
PROSITEi | View protein in PROSITE PS51332, B12_BINDING, 1 hit PS00544, METMALONYL_COA_MUTASE, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | MCM_RHOS4 | |
Accessioni | Q3J4D7Primary (citable) accession number: Q3J4D7 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 3, 2019 |
Last sequence update: | November 8, 2005 | |
Last modified: | February 10, 2021 | |
This is version 85 of the entry and version 1 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