ID A0A0F7FGB4_9CREN Unreviewed; 488 AA.
AC A0A0F7FGB4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Pyruvate carboxylase subunit A {ECO:0000313|EMBL:AKG38135.1};
DE EC=6.4.1.1 {ECO:0000313|EMBL:AKG38135.1};
GN ORFNames=MA03_00880 {ECO:0000313|EMBL:AKG38135.1};
OS Infirmifilum uzonense.
OC Archaea; Thermoproteota; Thermoprotei; Thermofilales; Thermofilaceae;
OC Infirmifilum.
OX NCBI_TaxID=1550241 {ECO:0000313|EMBL:AKG38135.1, ECO:0000313|Proteomes:UP000067434};
RN [1] {ECO:0000313|EMBL:AKG38135.1, ECO:0000313|Proteomes:UP000067434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1807-2 {ECO:0000313|EMBL:AKG38135.1,
RC ECO:0000313|Proteomes:UP000067434};
RX PubMed=26664700; DOI=10.1186/s40793-015-0105-y;
RA Toshchakov S.V., Korzhenkov A.A., Samarov N.I., Mazunin I.O., Mozhey O.I.,
RA Shmyr I.S., Derbikova K.S., Taranov E.A., Dominova I.N.,
RA Bonch-Osmolovskaya E.A., Patrushev M.V., Podosokorskaya O.A.,
RA Kublanov I.V.;
RT "Complete genome sequence of and proposal of Thermofilum uzonense sp. nov.
RT a novel hyperthermophilic crenarchaeon and emended description of the genus
RT Thermofilum.";
RL Stand. Genomic Sci. 10:122-122(2015).
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DR EMBL; CP009961; AKG38135.1; -; Genomic_DNA.
DR RefSeq; WP_052883469.1; NZ_CP009961.1.
DR AlphaFoldDB; A0A0F7FGB4; -.
DR STRING; 1550241.MA03_00880; -.
DR GeneID; 25400741; -.
DR KEGG; thf:MA03_00880; -.
DR PATRIC; fig|1550241.5.peg.178; -.
DR HOGENOM; CLU_000395_3_2_2; -.
DR OrthoDB; 31083at2157; -.
DR Proteomes; UP000067434; 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; 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};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AKG38135.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:AKG38135.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000067434}.
FT DOMAIN 4..449
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 123..320
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 488 AA; 54531 MW; FABDEE7DD1525F92 CRC64;
MGEYFDKILI ANRGEIAVRI IRTAKELGIK TVAVYSEADE NSLHVKLADE KVFIGPSEPR
ESYLNMEKII RAASSSGAEA IHPGYGFLSQ NPVFAEKVKE AGLTWIGPTP DVLKLAGDKI
SSRRFFAKAG IPIVPGTLDP VGLEEAEAKA EEIGYPVVVK PSGGGGGIGM FVAFSPEELK
EKIAKASRLA KAYFARTEVY LEKYFPRAKH IEVQILGDMH GKVIHLFERE CSVQRRFQKV
IEEAPSPSIT SEEREKLLTL AVKAAQSCNY VNAGTFEFLF DLNERRFYLL EVNTRIQVEH
PVTEMITGVD IVEQQLAIAS GEHLPSSLSD PSFRGHAIEA RIYAEDPASD FAPSPGSITR
LSLPAGPWIR VDSGVYEGFR VPEFYDSLLM KVIAWGHDRE SATRRLKRAL GELEIRGLKT
NRLFLIRILE DEDFVKGSYT TQILEKRELF KNLEEPVTTT MIQERAETKA EQTSKSISYW
RLLARAHV
//
