ID Q1QDX7_PSYCK Unreviewed; 704 AA.
AC Q1QDX7;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=3-methylcrotonoyl-CoA carboxylase, alpha subunit {ECO:0000313|EMBL:ABE74126.1};
DE EC=6.4.1.4 {ECO:0000313|EMBL:ABE74126.1};
GN OrderedLocusNames=Pcryo_0342 {ECO:0000313|EMBL:ABE74126.1};
OS Psychrobacter cryohalolentis (strain ATCC BAA-1226 / DSM 17306 / VKM B-2378
OS / K5).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=335284 {ECO:0000313|EMBL:ABE74126.1, ECO:0000313|Proteomes:UP000002425};
RN [1] {ECO:0000313|Proteomes:UP000002425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1226 / DSM 17306 / VKM B-2378 / K5
RC {ECO:0000313|Proteomes:UP000002425};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Sims D.R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Richardson P.;
RT "Complete sequence of chromosome of Psychrobacter cryohalolentis K5.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CP000323; ABE74126.1; -; Genomic_DNA.
DR RefSeq; WP_011512712.1; NC_007969.1.
DR AlphaFoldDB; Q1QDX7; -.
DR STRING; 335284.Pcryo_0342; -.
DR KEGG; pcr:Pcryo_0342; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_1_6; -.
DR Proteomes; UP000002425; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ABE74126.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 1..458
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..320
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 623..699
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 704 AA; 76299 MW; 2F37924129891402 CRC64;
MFSKILIANR GEIACRVAAT AKRLGVSTVA VYSDADREAK HVAVCDEAVY LGGSAPKDSY
LKGDAIIAIA KETGAQAIHP GYGFLSENAD FAQACQDADL VFIGPSADAI RAMGGKSESK
RLMETAGVPL IPGYHGENQD GAFLKQQADS IGYPVLIKAS AGGGGKGMRI VEQSSDFIDL
LESCRREAIT SFGNDQVLVE KYALKPRHIE IQVFGDTHGN YVHLFERDCS VQRRHQKVLE
EAPAPGVDAA MREAMGTAAI EAARAVNYFG AGTVEFIVEQ REGSMNFYFM EMNTRLQVEH
PVSEAISGVD LVEWQLLVAA GLPLPKKQEE LTINGHAIEA RICAENPDNG FLPATGTLFT
YQKPEHSTFV INKDGTGVRI DDGVREGDVI SPFYDSMIAK LIVHAPTREQ ALAKLDRALA
QTRIVGLPNN VAFLRYILNT ESFSQANLDT ALIEREREQL FDQHPLELST LAVTAIAQQL
ASESTTQGSD PFSKPTGFRA FSDYTRSFSL VYNEQSYKAL ISNWHNASCS DNKKGSDNLS
SFTLVIGKEV AKTQDNSNAN IAAQTESVYE GEVSYASIDA HNHTLWLDGA RINAQSWTNH
ETVYVFTDNG RDEITLVDIM AHVGEENAAV GSLKSPMPGQ VVAFKVAIGD SVKKGEPLAV
IEAMKIEHTI TAPTDGVVAE LLFGAGDLVA DGDELLRIDS QENQ
//
