ID Q2FNH4_METHJ Unreviewed; 492 AA.
AC Q2FNH4;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=Pyruvate carboxylase subunit A {ECO:0000313|EMBL:ABD42872.1};
DE EC=6.4.1.1 {ECO:0000313|EMBL:ABD42872.1};
GN OrderedLocusNames=Mhun_3190 {ECO:0000313|EMBL:ABD42872.1};
OS Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS JF-1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX NCBI_TaxID=323259 {ECO:0000313|EMBL:ABD42872.1, ECO:0000313|Proteomes:UP000001941};
RN [1] {ECO:0000313|Proteomes:UP000001941}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1
RC {ECO:0000313|Proteomes:UP000001941};
RX PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL Stand. Genomic Sci. 11:2-2(2016).
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DR EMBL; CP000254; ABD42872.1; -; Genomic_DNA.
DR RefSeq; WP_011450117.1; NC_007796.1.
DR AlphaFoldDB; Q2FNH4; -.
DR SMR; Q2FNH4; -.
DR STRING; 323259.Mhun_3190; -.
DR EnsemblBacteria; ABD42872; ABD42872; Mhun_3190.
DR GeneID; 3924655; -.
DR KEGG; mhu:Mhun_3190; -.
DR eggNOG; arCOG01590; Archaea.
DR HOGENOM; CLU_000395_3_2_2; -.
DR InParanoid; Q2FNH4; -.
DR OrthoDB; 31083at2157; -.
DR Proteomes; UP000001941; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC.
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};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ABD42872.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:ABD42872.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001941}.
FT DOMAIN 3..447
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 122..318
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 492 AA; 54575 MW; A58DDE4E8D39F34A CRC64;
MKYFEKILIA NRGEISIRVM RACRELGIDT VAIYSEADKD SLFVHYADEA FPVGPAPPSK
SYLNKERIIS VAKKAGAEAI HPGYGFLAEN AEFAKLCTEE GITFIGPKSK TIAAMGSKIR
SKQTMKGAGV PVLPGTDGGI DDLDMAATVA DSIGYPVIVK ASAGGGGIGM QIVHDPSEIE
SAIEGAMRIA ESAFGDRTVF IEKYLQKPRH VEVQVFCDEH DNRIHMFERE CSIQRRHQKL
IEEAPCPVMT PELRERMTNS ALRVAEAVDY VNAGTVEFLY DNGEYYFMEM NTRLQVEHTI
TELVTGIDIV KEQIIVASGD PIEYGQEDIT LRGHAIECRI NAEDPMNNFA ADPGKITRYR
SPGGPGIRLD SGIHAGYTIP PFYDSMISKL CAWGMSREYA IARMRRAIYE YVILGVKTTL
PLHHAIIHNP EFIAGNTHTH FLQEEHISRT LKRYIQEEET RMTQLATPLR ADKKVAAIAA
GLVAVIEQNK QN
//
