ID A0A1R1MMT4_9BACT Unreviewed; 472 AA.
AC A0A1R1MMT4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Acetyl-CoA carboxylase biotin carboxylase subunit {ECO:0000313|EMBL:OMH41131.1};
GN ORFNames=BLW93_01185 {ECO:0000313|EMBL:OMH41131.1};
OS Desulfurobacterium indicum.
OC Bacteria; Aquificota; Aquificae; Desulfurobacteriales;
OC Desulfurobacteriaceae; Desulfurobacterium.
OX NCBI_TaxID=1914305 {ECO:0000313|EMBL:OMH41131.1, ECO:0000313|Proteomes:UP000187408};
RN [1] {ECO:0000313|EMBL:OMH41131.1, ECO:0000313|Proteomes:UP000187408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K6013 {ECO:0000313|EMBL:OMH41131.1,
RC ECO:0000313|Proteomes:UP000187408};
RA Cao J., Shao Z., Alain K., Jebbar M.;
RT "Genome sequence of a sulfur-reducing bacterium Desulfurobacterium indicum
RT K6013.";
RL Submitted (OCT-2016) 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:OMH41131.1}.
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DR EMBL; MOEN01000003; OMH41131.1; -; Genomic_DNA.
DR RefSeq; WP_076712288.1; NZ_MOEN01000003.1.
DR AlphaFoldDB; A0A1R1MMT4; -.
DR STRING; 1914305.BLW93_01185; -.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000187408; 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; IPR004549; Acetyl_CoA_COase_biotin_COase.
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 NCBIfam; TIGR00514; accC; 1.
DR PANTHER; PTHR48095:SF1; BIOTIN CARBOXYLASE; 1.
DR PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 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 SMART; SM01209; GARS_A; 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}; Reference proteome {ECO:0000313|Proteomes:UP000187408}.
FT DOMAIN 1..445
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 472 AA; 53155 MW; CC82038E03A78BBD CRC64;
MFKKILIANR SEVATRVIRA CKELGIKTVA IYSEADVNSL HVKKADEAYM IHGDPVKAYL
NYYKIVDIAR RAGVDAIHPG YGFLSERPDF AEYCRKKGVE FIGPSVEHLK MFGSKLKAKK
VMKELGVPVA EGSDRAVSDI EEAKELAKKI GYPVMIKASH GGGGRGLRVA RNEKELVSQF
KTAVAEAEAA FGKGEVFIEK YIEEPRHIEI QIIADKNGNV VHLGERDCSM QRRHQKVLEI
APSPVLTKRQ REKLGQICVR VAREIGYYGV GTWEFLMDKY GKFYFMEVNP RLQVEHTITE
AVTGIDIVQE QIRIAAGMNL SFSQKSVNIY GFAMQFRINA EDVTRDFVPS PGTVTAYYSP
GGIGVRIDGV VYKGYKIPPY YDSMIAKLIV WGRNWDEVIR RSRRALDEFV IRGVPTTIPF
FKKILNDPEF IHGKFDTSFI DRKIKEFTFI KEPDPEILAL ALSAAIAAHH GL
//