ID M3CIR7_LEPIR Unreviewed; 487 AA.
AC M3CIR7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Putative acetyl-CoA carboxylase, biotin carboxylase subunit {ECO:0000313|EMBL:EMF41309.1};
GN ORFNames=LEP1GSC067_0743 {ECO:0000313|EMBL:EMF41309.1};
OS Leptospira interrogans serovar Lora str. TE 1992.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1193028 {ECO:0000313|EMBL:EMF41309.1, ECO:0000313|Proteomes:UP000011754};
RN [1] {ECO:0000313|EMBL:EMF41309.1, ECO:0000313|Proteomes:UP000011754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TE 1992 {ECO:0000313|EMBL:EMF41309.1,
RC ECO:0000313|Proteomes:UP000011754};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Hartskeerl R.A., Ahmed A.,
RA van der Linden H., Goris M.G.A., Vinetz J.M., Sutton G.G., Nierman W.C.,
RA Fouts D.E.;
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
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:EMF41309.1}.
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DR EMBL; AKWW02000062; EMF41309.1; -; Genomic_DNA.
DR AlphaFoldDB; M3CIR7; -.
DR Proteomes; UP000011754; 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 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; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_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; 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 PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 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 1..448
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 487 AA; 54258 MW; E96DC8C75FB21095 CRC64;
MISKLLIANR GEIAVRVIRT CKKLGIKTVA IYSDADRDSP HVKLADESVY VGEPSPASSY
LNISNILEAI KKTKTDAVHP GYGFLSEKSE FAKALEKENV LFLGPSPESM ELMGDKINSR
IKMEASGVPV VPGYNGQNQD PKILQKEAEK IGYPLMIKAT AGGGGKGMKR VYKSEEFLFA
LESAQREAQK AFGDGTVFLE KYVETPRHIE VQVFGDKHGN VMHLFERECS IQRRHQKVIE
ESPAPNLPIS LRDEICRVAV KAAQSIGYVG AGTVEFILGR DSKFYFLEMN TRLQVEHPVT
EYITGQDLVE WQIQVAEGKK LSELTKGKTV IQNGHAIEAR IYAEDPENNF LPSTGILEYI
EFPDREFLRV DTGVETGSEI TVYYDPMIAK MIAWGKTREE CTARLKESID STVIFGPVTN
TFYLSGILSH EEFKKGNTHT HFLEEQTILF TPEKDVQADA FSFAAAALSE KKKSQGIWEA
VGPGGFW
//
