ID J2Z1F0_9LACO Unreviewed; 437 AA.
AC J2Z1F0;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Putative acetyl-CoA carboxylase, biotin carboxylase subunit {ECO:0000313|EMBL:EJN54238.1};
GN ORFNames=A11Y_151236 {ECO:0000313|EMBL:EJN54238.1};
OS Loigolactobacillus coryniformis subsp. coryniformis CECT 5711.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Loigolactobacillus.
OX NCBI_TaxID=1185325 {ECO:0000313|EMBL:EJN54238.1, ECO:0000313|Proteomes:UP000007271};
RN [1] {ECO:0000313|EMBL:EJN54238.1, ECO:0000313|Proteomes:UP000007271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT5711 {ECO:0000313|Proteomes:UP000007271};
RA Rodriguez J.M.;
RT "Complete Genome Sequence of Lactobacillus coryniformis CECT5711.";
RL Submitted (MAY-2012) 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:EJN54238.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKFP01000102; EJN54238.1; -; Genomic_DNA.
DR RefSeq; WP_003680339.1; NZ_AKFP01000102.1.
DR AlphaFoldDB; J2Z1F0; -.
DR STRING; 1185325.A11Y_151236; -.
DR PATRIC; fig|1185325.3.peg.2523; -.
DR Proteomes; UP000007271; 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:UniProtKB-KW.
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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000007271}.
FT DOMAIN 1..435
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 437 AA; 46870 MW; C1610A2336AE4B27 CRC64;
MKKVLIANRG EIAVRIIRAC RELNIPTVAI YSTADKKALH VQLADEAICV GPADPQKSYL
NIDNIVAAAT TMAADAVHPG YGFLSENAEF AQRCEEQGLV FIGPSAKVIA QMGDKAAARE
LMQAAGVPVI PGGRQGFTNQ KVGAKVAADI GYPVMLKAAA GGGGKGMRVV MAAKQFGHEF
QLAQSEAEKS FANGEMYLEK FIAHPRHIEV QIMGDTYGNV LTLGERDCSL QQNHQKMVEE
APSDVLDAAT RKQMLATSVT AAKAIHYVGA GTIEFLYAGP GQFYFMEMNT RVQVEHPITE
LITKEDIVAW QLKIASDQAL PTVTPAINGH AVECRVNAQT PGVITGLHLP GGNGVRVDTA
LYQGYAVPPD YDAMIAKIIV YAADRTTAIA KMRAAIDETV ISGIQTNLDF LTELLAAPDY
LADNVNITFI DDFVAAH
//
