ID A0A101D336_9GAMM Unreviewed; 683 AA.
AC A0A101D336;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Methylcrotonoyl-CoA carboxylase, biotin carboxylase subunit {ECO:0000313|EMBL:KUJ88098.1};
DE EC=6.4.1.4 {ECO:0000313|EMBL:KUJ88098.1};
GN Name=accA {ECO:0000313|EMBL:KUJ88098.1};
GN ORFNames=XD36_1468 {ECO:0000313|EMBL:KUJ88098.1};
OS Halomonas sp. 54_146.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1635257 {ECO:0000313|EMBL:KUJ88098.1, ECO:0000313|Proteomes:UP000053192};
RN [1] {ECO:0000313|Proteomes:UP000053192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUJ88098.1}.
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DR EMBL; LGEN01000013; KUJ88098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101D336; -.
DR STRING; 1635257.XD36_1468; -.
DR PATRIC; fig|1635257.4.peg.834; -.
DR Proteomes; UP000053192; Unassembled WGS sequence.
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; 3.30.700.40; -; 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:KUJ88098.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 7..462
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 126..327
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 607..680
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 683 AA; 73521 MW; 0B07BC5A44F5A32F CRC64;
MTFTPTKFDT LLVANRGEIA CRVMRTARRM GLKTVAVYSD ADASARHVRE ADEAVRLGPA
AARESYLNID AVIDAAKRTG TGAIHPGYGF LSENGSFVKA LEDAGITFVG PPASAIAAMG
DKSAAKARMA NAGVPLVPGY HGDDQDDALL RAEADKIGYP VMLKASAGGG GKGMRVVESG
DGFQAALDGC RRESKAAFGD DRMLIEKYLV QPRHVEVQVF CDRHGNGVYL FERDCSVQRR
HQKVIEEAPA PGMTAELRSA MGDAAVRAAQ EIGYVGAGTV EFLLDGSPGQ DGAFYFMEMN
TRLQVEHPVT EMITGQDLVE WQLRVAMGEP LPCRQDELTI TGHSFEARIY AEDPDQDFLP
ATGLLTRFAL DLEGAGLSAD QVRLDSGVES GDAVSMHYDP MLAKLIVHGA DRDAALATLN
RALAALDVQG VVTNRAFLMR LATHPGFKNV ELDTRFIERN EATLFAPRTY SMEAYASAAL
IGLHQLAQEC ETDSPWDRHD GFRLNAPHTI RIALCNPASA QAPDSDDAVV IVEGKRSAGE
SLWNLTIGDE TLTASLQPLT GDAVAVTLNG HRRRLQARRD GHVVVMADPS GETRLFWRRI
DAIDHGHHEA ESTLTAPMNG TVVALLVEPG VAVEKGMPLM VMEAMKMEHT MTAPADGSVE
AFHFQAGDTV SQGAVLLDFA ANE
//