ID A0A0M2CRJ9_9MICC Unreviewed; 597 AA.
AC A0A0M2CRJ9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=H488_0115780 {ECO:0000313|EMBL:EYT48636.1};
OS Kocuria sp. UCD-OTCP.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=1292021 {ECO:0000313|EMBL:EYT48636.1, ECO:0000313|Proteomes:UP000033173};
RN [1] {ECO:0000313|EMBL:EYT48636.1, ECO:0000313|Proteomes:UP000033173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-OTCP {ECO:0000313|EMBL:EYT48636.1,
RC ECO:0000313|Proteomes:UP000033173};
RX PubMed=23661474;
RA Coil D.A., Doctor J.I., Lang J.M., Darling A.E., Eisen J.A.;
RT "Draft Genome Sequence of Kocuria sp. Strain UCD-OTCP (Phylum
RT Actinobacteria).";
RL Genome Announc. 1:E00172-13(2013).
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:EYT48636.1}.
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DR EMBL; AOSQ01000038; EYT48636.1; -; Genomic_DNA.
DR RefSeq; WP_017834227.1; NZ_AOSQ01000038.1.
DR AlphaFoldDB; A0A0M2CRJ9; -.
DR HOGENOM; CLU_000395_3_1_11; -.
DR Proteomes; UP000033173; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
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; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
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; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 13..456
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 132..329
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 521..597
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 501..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 62577 MW; 65B3B43E4A0C322E CRC64;
MTGKNPADGA IRPITKVLVA NRGEIAVRVI RAARDEGIAS VAVYADPDRD ALHARTADEA
YGLGGSTAAD SYLVIDKILD VAARSGADAV HPGYGFLSEN AEFALAVLEA GLTWIGPPPA
AIAKLGDKVA ARHIAEKVGA PQVPGTTDPV GSAEEVLAFA DEHGLPLAIK AAFGGGGRGI
KVVRNRDDIP ELYESAVREA TAAFGRGDCF VERFLDAPRH VETQCLADAH GHVVVVSTRD
CSLQRRNQKL VEEAPAPFLS EEQNRLLYAS SKAILREAGY QGAGTCEFLV GQDGTITFLE
VNTRLQVEHP VSEEVTGIDL VREQFRLARG EALGYDDPEV RGHSIEFRIN GEDPGRHFMP
SPGTIAALDL PGGPGVRVDS GVQAGETVGG NFDSMLAKLI VTGATRQQAL ERSRRALAEL
RIEGMPTVVP FHRAVVADPA FAPADGAPFS VHTRWIETEF DNTIPPFEGV PQAGPEAEER
QAIVVEVSGK RLEVVLPALP GTAKPNGAAA KPRKSRSARG GGTAAASGDS LSSPMQGTIV
KIAVDNGDEV AEGDLVLVLE AMKMEQPLTA HKSGTVSGLS VSPGDTVSAG AVLATIS
//
