ID G7WLD2_METH6 Unreviewed; 495 AA.
AC G7WLD2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Pyruvate carboxylase subunit A {ECO:0000313|EMBL:AET64235.1};
GN OrderedLocusNames=Mhar_0863 {ECO:0000313|EMBL:AET64235.1};
OS Methanothrix harundinacea (strain 6Ac) (Methanosaeta harundinacea).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanotrichales; Methanotrichaceae; Methanothrix.
OX NCBI_TaxID=1110509 {ECO:0000313|EMBL:AET64235.1, ECO:0000313|Proteomes:UP000005877};
RN [1] {ECO:0000313|EMBL:AET64235.1, ECO:0000313|Proteomes:UP000005877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6Ac {ECO:0000313|EMBL:AET64235.1,
RC ECO:0000313|Proteomes:UP000005877};
RX PubMed=22590603; DOI=10.1371/journal.pone.0036756;
RA Zhu J., Zheng H., Ai G., Zhang G., Liu D., Liu X., Dong X.;
RT "The genome characteristics and predicted function of methyl-group
RT oxidation pathway in the obligate aceticlastic methanogens, Methanosaeta
RT spp.";
RL PLoS ONE 7:E36756-E36756(2012).
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DR EMBL; CP003117; AET64235.1; -; Genomic_DNA.
DR RefSeq; WP_014586420.1; NC_017527.1.
DR AlphaFoldDB; G7WLD2; -.
DR STRING; 1110509.Mhar_0863; -.
DR GeneID; 12510032; -.
DR KEGG; mhi:Mhar_0863; -.
DR PATRIC; fig|1110509.7.peg.959; -.
DR HOGENOM; CLU_000395_3_2_2; -.
DR OrthoDB; 31083at2157; -.
DR Proteomes; UP000005877; Chromosome.
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 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}; Pyruvate {ECO:0000313|EMBL:AET64235.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005877}.
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 495 AA; 54616 MW; 69CADE83E446BAD1 CRC64;
MFQKILIANR GEIAIRIMRA CRELGISTVA VYSEADRNAL FAKYADEAVF VGPSPASQSY
LRIDRILEAA EETGAEAIHP GYGFLSENPK FARACEEKGV VFIGPTSSSI DRMGSKIAAR
DIMKSAGVPI VPGSEGGISN PAEAMDLVEA IGYPVMLKPA AGGGGIGMKI VWEEKDLAPA
LDSARSIARS AFSDETVYIE KYLTEPRHIE FQILADSKGK TIYVSDRECS IQRRHQKLIE
ESPSPIMTPE LREEMGSIAV RAAEAIDYRS AGTVEFMYSK GEYYFLEMNT RLQVEHPITE
MVTSVDLAKE QIRIAAGEPL AYSQDEIEIR GWAIECRVNA EDPLNDFAPS PGRIKRYRSP
GGPGIRVDSG VYAGFLIPPY YDSMISKVVA MGRDRNEAIA RMERALYEYI VTGVKTNINF
HLAVLRHERF RRGDINTNFL KEEAIMEEVK KVTEAEREKE LSLASALGAD TRKVAAISAA
VGAYMSQREN PGSEE
//
