ID G4F364_9GAMM Unreviewed; 684 AA.
AC G4F364;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Methylcrotonoyl-CoA carboxylase, biotin carboxylase subunit {ECO:0000313|EMBL:EHA16917.1};
GN ORFNames=HAL1_04052 {ECO:0000313|EMBL:EHA16917.1};
OS Halomonas sp. HAL1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=550984 {ECO:0000313|EMBL:EHA16917.1, ECO:0000313|Proteomes:UP000005692};
RN [1] {ECO:0000313|EMBL:EHA16917.1, ECO:0000313|Proteomes:UP000005692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain {ECO:0000313|Proteomes:UP000005692};
RX PubMed=22156396; DOI=10.1128/JB.06359-11;
RA Lin Y., Fan H., Hao X., Johnstone L., Hu Y., Wei G., Alwathnani H.A.,
RA Wang G., Rensing C.;
RT "Draft Genome Sequence of Halomonas sp. Strain HAL1, a Moderately
RT Halophilic Arsenite-Oxidizing Bacterium Isolated from Gold-Mine Soil.";
RL J. Bacteriol. 194:199-200(2012).
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:EHA16917.1}.
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DR EMBL; AGIB01000017; EHA16917.1; -; Genomic_DNA.
DR RefSeq; WP_008956740.1; NZ_CP130610.1.
DR AlphaFoldDB; G4F364; -.
DR PATRIC; fig|550984.5.peg.791; -.
DR Proteomes; UP000005692; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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 SMART; SM01209; GARS_A; 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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 12..463
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 131..328
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 608..681
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 684 AA; 73905 MW; 99EB665894FEDCD3 CRC64;
MKKHEKAART TPFDTLLIAN RGEIACRVMR TARRMGLKTV AVYSDADASA LHVREADEAV
RLGPAAARES YLNIDAVIEA AKRTGTGAIH PGYGFLSENG TFVKALEEAG ITFVGPPASA
IAAMGDKSAA KARMANAGVP LVPGYHGDDQ DDALLRSEAD KIGYPVMLKA SAGGGGKGMR
VVESSDGFQA ALDGCRRESK AAFGDDRMLI EKYLVQPRHV EVQVFCDRHG NGVYLFERDC
SVQRRHQKVI EEAPAPGMTA ELRCAMGDAA VRAAQEIGYV GAGTVEFLLD ADGSFYFMEM
NTRLQVEHPV TEMITGQDLV EWQLRVAMGE PLPCTQDELT ITGHSFEARI YAEDPEQDFL
PATGLLTRFA LDLEGAGLSD DQVRLDSGVE SGDAVSMHYD PMLAKLIVHG ADRDAALATL
NRALAALDVQ GVVTNRAFLM RLATHPGFKN VELDTRFIER NEATLFAPRT YSTEAYASAA
LIGLNQLAQE CESDSPWDRH DGFRLNAPHT IRIALCDPTN IQAADSDDAV VIVEGKRNAA
ESLWNLTIGD ETLTASLQPL TGDAVAVTLN GHRRRLQACR DGHVVVMADS SGETRLFWRR
IDAIDHGHHE AESTLTAPMN GTVVALLVEP GVTVEKGMPL MVMEAMKMEH TMTAPADGSV
ETFHFKAGDT VNQGAVLLDF AANE
//
