ID A0A1M5LHA0_9FLAO Unreviewed; 480 AA.
AC A0A1M5LHA0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Propionyl-CoA carboxylase alpha chain {ECO:0000313|EMBL:SHG64421.1};
GN ORFNames=SAMN05443373_10392 {ECO:0000313|EMBL:SHG64421.1};
OS Flavobacterium granuli.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=280093 {ECO:0000313|EMBL:SHG64421.1, ECO:0000313|Proteomes:UP000184384};
RN [1] {ECO:0000313|Proteomes:UP000184384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19729 {ECO:0000313|Proteomes:UP000184384};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FQWO01000003; SHG64421.1; -; Genomic_DNA.
DR RefSeq; WP_072941348.1; NZ_PVUB01000004.1.
DR AlphaFoldDB; A0A1M5LHA0; -.
DR STRING; 280093.SAMN05443373_10392; -.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000184384; 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..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 480 AA; 53453 MW; F73B941C1A8B1BF2 CRC64;
MKKILVANRG EIAIRVTKTA QKMGIKTVAV YSTIDRNAPH VKFADEAVWI GESPSNQSYL
LGDKIIEVAK SLGVDAIHPG YGFLSENAEF AEKAEQNNII FIGPKSKAIH IMGSKLAAKE
AVKVYNIPMV PGLDEAITDI EKAKAAATEI GFPILIKASA GGGGKGMRVV ENAAEFESQM
KRAISEAINA FGDGSVFIEK YVASPRHIEI QIMADSHGNI LYLFERECSI QRRHQKVVEE
APSAVLTPDL RRKMGEAAVL VAKSCDYLGA GTVEFLLDEH NNFYFLEMNT RLQVEHPVTE
WITGLDLVEL QIKIARGEEL EIQQEDLKIK GHALELRVYA EDPMNDFLPS VGHLGVYQLP
VGEGIRVDNG FEQGMDIPIY YDPMLAKLIT YGETREEAIQ IMLKAIEGYL VEGVQTTLPF
GKFVFEHEAF RSGNFDTHFV KKYYSADLLK NQLEKEAEIA AMIALKQYFE DQKIVRLPNQ
//
