ID A0A1Z5IHW3_9LACO Unreviewed; 458 AA.
AC A0A1Z5IHW3;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Acetyl-CoA carboxylase, biotin carboxylase subunit {ECO:0000313|EMBL:GAX01162.1};
GN Name=accC_2 {ECO:0000313|EMBL:GAX01162.1};
GN ORFNames=IWT126_01187 {ECO:0000313|EMBL:GAX01162.1};
OS Secundilactobacillus silagei JCM 19001.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Secundilactobacillus.
OX NCBI_TaxID=1302250 {ECO:0000313|EMBL:GAX01162.1, ECO:0000313|Proteomes:UP000198402};
RN [1] {ECO:0000313|EMBL:GAX01162.1, ECO:0000313|Proteomes:UP000198402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IWT126 {ECO:0000313|EMBL:GAX01162.1,
RC ECO:0000313|Proteomes:UP000198402};
RA Tohno M., Tanizawa Y., Arita M.;
RT "Draft genome sequences of new species of the genus Lactobacillus isolated
RT from orchardgrass silage.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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:GAX01162.1}.
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DR EMBL; BCMG01000005; GAX01162.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5IHW3; -.
DR STRING; 1302250.GCA_001313225_01820; -.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000198402; 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; 3.40.50.20; -; 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; 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}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW 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}.
FT DOMAIN 1..446
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 458 AA; 50051 MW; 62209EEDCFF39C3E CRC64;
MFKKVLIANR GEIAVRIIRA LRELNIQSVA IYSTADADAQ YVKLADEAIC VGGPQPADSY
LNMQNIVSAA VLTGAEAIHP GYGFLSENAE FAELCESCQI TFIGPKPQTI SLMGNKANAR
IQMQAGKVPV IPGSTGFLKD ETDAVKVAGE VGYPVMLKAA SGGGGKGIRQ VANEHEMRAA
YQSATKEAQL SFGDQRMYLE KIISPAKHIE VQVFADQFGH VTAFPERDCS LQRRQQKVLE
LSPCPEMSAP ERRQLQQIAI RATKAIDYLN TGTIEFLMDA KHQFYFMEMN TRIQVEHPIT
EAVTGVDLVK KQVRVAAGEP LSFDQADLKV QGFAVEARVN AEDPALNFMP QAGVIKQLKL
PGGPGIRVDN GIQAGDMISP FYDSMIVKII AHAPTYQEAL KKLSEALAEF ELVGIATNQN
FLQALLADPV VQQGTATTAY VTERFMPIFM KRNVQEVS
//
