Q54KE6 (MCCA_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
Short name=MCCase subunit alpha
EC=6.4.1.4

Alternative name(s):
3-methylcrotonyl-CoA carboxylase 1
3-methylcrotonyl-CoA carboxylase biotin-containing subunit
3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha

Gene names

Name:	mccA
Synonyms:	mccc1
ORF Names:	DDB_G0287377

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	699 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + 3-methylcrotonoyl-CoA + HCO3- = ADP + phosphate + 3-methylglutaconyl-CoA.
Cofactor	Binds 2 manganese ions per subunit By similarity. Biotin By similarity.
Pathway	Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 2/3.
Subunit structure	Probably a dodecamer composed of six biotin-containing alpha subunits and six beta subunits By similarity.
Subcellular location	Mitochondrion matrix By similarity.
Sequence similarities	Contains 1 ATP-grasp domain. Contains 1 biotin carboxylation domain. Contains 1 biotinyl-binding domain.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	ATP-binding Biotin Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	leucine catabolic process Inferred from sequence or structural similarity. Source: dictyBase
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW biotin carboxylase activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: InterPro methylcrotonoyl-CoA carboxylase activity Inferred from sequence or structural similarity. Source: dictyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 699		Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial		PRO_0000327665
Regions
	Domain	30 – 475	446	Biotin carboxylation
	Domain	148 – 345	198	ATP-grasp
	Domain	616 – 698	83	Biotinyl-binding
Sites
	Active site	320	1	By similarity
	Binding site	144	1	ATP By similarity
	Binding site	228	1	ATP By similarity
	Binding site	263	1	ATP By similarity
Amino acid modifications
	Modified residue	665	1	N6-biotinyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54KE6 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: B1FD14E7E286A96D	FASTA	699	77,089
	10 20 30 40 50 60 MFSLGKLVKK DAFFYRYITN VNKDLKIKPI TKILIANRGE IACRVMRTAK SKGVKTVAVY 70 80 90 100 110 120 SEADKNSLHV SMADESYLIG PAAAKESYLC GNKIIDVAKR SGAQAIHPGY GFLSENSDFA 130 140 150 160 170 180 DLCEREGIIF IGPPSDAIKA MGSKSASKDI MIKAGVPTIP GYHGEDQSMS VLKSEAAKIG 190 200 210 220 230 240 YPVLIKAVMG GGGKGMRIVE REEDLEDGVE SSKREATASF GDSRVLVEKY LVHPRHVEIQ 250 260 270 280 290 300 VFADRHGNCV HLFERDCSVQ RRHQKIIEEA PAPHLSEELR KKMGDAAVAA AKAVGYVGAG 310 320 330 340 350 360 TVEFILSADN SFFFMEMNTR LQVEHPITEM ITKQDLVEWQ LKVAESQTLP MEQEQLKIHG 370 380 390 400 410 420 HSFEARIYAE NPDSDFLPGT GKLAHLSTPT PSDTLRVETG VRQGDEVSVY YDPMIAKLVV 430 440 450 460 470 480 WDQDREKALR YLRNALDEYH IIGLNTNISF LKRLSTHPSF MAGEVETGFI PIHRESLMAP 490 500 510 520 530 540 QAPMSDDSLA LAATSLLLKE ITQQKSKEDP NSPWSSLGGF RINHNLKKQV KFNQKDNKVV 550 560 570 580 590 600 VNVEFIGGGG AAANGKHNFK VTLDNGNVVE VLDAKLNQNN ETISAHVNGR FYNNIKSVIV 610 620 630 640 650 660 KDTLTIFNEG QQYQLDIPQD VKPKGADGVL GSLVSPMPGK ITKVMVNVGD MVKKGQPILL 670 680 690 MEAMKMEHTI RSPIDGKVES LPYNVNEIVE DKKTLAVIV

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000100 Genomic DNA. Translation: EAL63756.1.
RefSeq	XP_637277.1. XM_632185.1.
3D structure databases
HSSP	HSSP built from PDB template 1BNC based on UniProtKB P24182.
ProteinModelPortal	Q54KE6.
ModBase	Search...
Protein-protein interaction databases
STRING	Q54KE6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0230065; DDB0230065; DDB_G0287377.
GeneID	8626108.
GenomeReviews	Gene locus mccA in contig CM000154_GR.
KEGG	ddi:DDB_G0287377.
Organism-specific databases
dictyBase	DDB_G0287377. mccA.
Phylogenomic databases
eggNOG	KOG0238.
GeneTree	EPrGT00050000001985.
HOGENOM	HBG535236.
OMA	HLSTPRA.
PhylomeDB	Q54KE6.
ProtClustDB	CLSZ2430009.
Family and domain databases
InterPro	IPR011761. ATP-grasp. IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR001882. Biotin_BS. IPR011764. Biotin_carboxylation_dom. IPR005482. Biotin_COase_C. IPR000089. Biotin_lipoyl. IPR005479. CarbamoylP_synth_lsu_ATP-bd. IPR005481. CarbamoylP_synth_lsu_N. IPR013817. Pre-ATP_grasp. IPR016185. PreATP-grasp-like. IPR011054. Rudment_hybrid_motif. IPR011053. Single_hybrid_motif. [Graphical view]
Gene3D	G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit. G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit. G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.
KO	K01968.
Pfam	PF02785. Biotin_carb_C. 1 hit. PF00364. Biotin_lipoyl. 1 hit. PF00289. CPSase_L_chain. 1 hit. PF02786. CPSase_L_D2. 1 hit. [Graphical view]
SMART	SM00878. Biotin_carb_C. 1 hit. [Graphical view]
SUPFAM	SSF51230. Hybrid_motif. 1 hit. SSF52440. PreATP-grasp-like. 1 hit. SSF51246. Rudmnt_hyb_motif. 1 hit.
PROSITE	PS50975. ATP_GRASP. 1 hit. PS50979. BC. 1 hit. PS00188. BIOTIN. 1 hit. PS50968. BIOTINYL_LIPOYL. 1 hit. PS00867. CPSASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MCCA_DICDI

Accession

Primary (citable) accession number: Q54KE6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	November 16, 2011
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)