ID M2XSY8_9MICC Unreviewed; 581 AA.
AC M2XSY8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Biotin carboxylase of acetyl-CoA carboxylase {ECO:0000313|EMBL:EME35923.1};
GN ORFNames=C884_00924 {ECO:0000313|EMBL:EME35923.1};
OS Kocuria palustris PEL.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=1236550 {ECO:0000313|EMBL:EME35923.1, ECO:0000313|Proteomes:UP000009877};
RN [1] {ECO:0000313|EMBL:EME35923.1, ECO:0000313|Proteomes:UP000009877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEL {ECO:0000313|EMBL:EME35923.1,
RC ECO:0000313|Proteomes:UP000009877};
RX PubMed=24504000;
RA Sharma G., Khatri I., Subramanian S.;
RT "Draft Genome Sequence of Kocuria palustris PEL.";
RL Genome Announc. 2:e01261-13(2014).
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:EME35923.1}.
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DR EMBL; ANHZ02000019; EME35923.1; -; Genomic_DNA.
DR RefSeq; WP_006215353.1; NZ_ANHZ02000019.1.
DR AlphaFoldDB; M2XSY8; -.
DR STRING; 71999.KPaMU14_00160; -.
DR Proteomes; UP000009877; 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:SF126; BIOTIN CARBOXYLASE; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 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}; Reference proteome {ECO:0000313|Proteomes:UP000009877}.
FT DOMAIN 1..444
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 505..580
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 581 AA; 61016 MW; E544B39E350EE522 CRC64;
MQKVLIANRG EIAVRIIHAC AEAGLSSVAV YADPDADAPH VHLADEAYAL EGTSPTETYL
DQEAILAIAQ RAAADAVHPG YGFLSENASF ARGVIDAGLT WIGPKPETIE KLGDKVQARD
IARTVGAPLV PGTDGPVASG AEATAFAEEH GLPVIIKAAH GGGGRGMRVV RELSEVEDAF
ASAAREAQSA FGRPECFVER FLDEPRHVEA QVVCDSHGGV AVLGTRDCSL QRRHQKLVEE
APAPFLSDEQ RERIHTAAAE ICREAGYVGV GTAEFLVGRD GLISFLEVNT RLQVEHPITE
EVYGADLVQL QLLVADGGHL PEGLGAQPQG HAFEFRINAE DPGRGFLPGG GRIEAIDAPT
GPGIRLDSGV RAGQEVATTF DSMLLKLIVH GADRQAALRR ARRALAEIRI HGVATTVPFH
RAAVEAPEFA AETAGDFTVH TAWIENEFAE RLSADDGYAA DYLRAAELGR SRFSVDIDGR
RVMLGVPKAL AAALESGGQA SSSGSAETDD DGAIKAGVGG TVLKWLVEEG AQVQAGDDLL
VLEVMKTESK VAAPCAGTLS ERGAAEGDAV TAGQVLGRIT S
//
