ID A0A2V3JPM4_9EURY Unreviewed; 494 AA.
AC A0A2V3JPM4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Acetyl-CoA carboxylase biotin carboxylase subunit {ECO:0000313|EMBL:PXF62174.1};
GN Name=accC {ECO:0000313|EMBL:PXF62174.1};
GN ORFNames=C4B59_00755 {ECO:0000313|EMBL:PXF62174.1};
OS ANME-2 cluster archaeon.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinales incertae sedis; ANME-2 cluster.
OX NCBI_TaxID=2056317 {ECO:0000313|EMBL:PXF62174.1, ECO:0000313|Proteomes:UP000248329};
RN [1] {ECO:0000313|EMBL:PXF62174.1, ECO:0000313|Proteomes:UP000248329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E20ANME2 {ECO:0000313|EMBL:PXF62174.1};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) 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:PXF62174.1}.
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DR EMBL; PQXF01000001; PXF62174.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V3JPM4; -.
DR Proteomes; UP000248329; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000248329}.
FT DOMAIN 1..445
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 494 AA; 54012 MW; D1A1EA1CC73C391D CRC64;
MFNTILVANR GEIAIRAMRA CHEMGIMTVA VYSEADKHAL FAKYADVAHC IGPPPTSQSY
LMIDRILDVA EKTGAEAIHP GYGFLSENSV FARECEKAGI VFIGPSGKCM EASGSKIAAR
KAMEKAGIPI IPGISAGIDD LESTLDDAEK IGYPVIVKAS AGGGGIGMKI ANDASELQGA
IDSTQAVAES VFGDATIFME KYLHQPRHIE FQILADSHGN TIHLNERECS IQRRHQKLIE
ESPSPVMTPE LREEMGRTAI GAAEAFDYTN AGTVEFIYSD GDFYFLEMNT RLQVEHPITE
QVTGLDIVRR QIRIAAGEEL DRRQEDIGIN GWAIECRINA EDPMNDFAPS PGRLTRYRSP
GGPGIRVDSG VYTGYTISPY YDSMVSKLIS WGENRLEAIE RMRRALYEYI IIGVTTNIPF
HKAVLKNPHF IRAELTTHFI DDFDIPAEVA VVVEQEKVKG ATLASAIGSD DRKVAAITAA
VQTYMGGSTQ IADN
//
