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Database: UniProt
Entry: A0A101D336_9GAMM
LinkDB: A0A101D336_9GAMM
Original site: A0A101D336_9GAMM 
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
//
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