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Database: UniProt
Entry: R7HP40_9BACT
LinkDB: R7HP40_9BACT
Original site: R7HP40_9BACT 
ID   R7HP40_9BACT            Unreviewed;       623 AA.
AC   R7HP40;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Putative pyruvate carboxylase subunit B {ECO:0000313|EMBL:CDE40698.1};
GN   ORFNames=BN585_01636 {ECO:0000313|EMBL:CDE40698.1};
OS   Prevotella sp. CAG:279.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262924 {ECO:0000313|EMBL:CDE40698.1, ECO:0000313|Proteomes:UP000018375};
RN   [1] {ECO:0000313|EMBL:CDE40698.1, ECO:0000313|Proteomes:UP000018375}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:279 {ECO:0000313|Proteomes:UP000018375};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDE40698.1}.
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DR   EMBL; CBIX010000054; CDE40698.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7HP40; -.
DR   Proteomes; UP000018375; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR000891; PYR_CT.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR45266; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR   PANTHER; PTHR45266:SF3; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF02436; PYC_OADA; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   4: Predicted;
KW   Pyruvate {ECO:0000313|EMBL:CDE40698.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018375}.
FT   DOMAIN          5..292
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   DOMAIN          546..622
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   623 AA;  67992 MW;  0F56F517BBE289D2 CRC64;
     MSRSLKVRDL TLRDGQQSLF ATRMKQESID KLLPLYKDAG FYAMEVWGGA VPDSVMRYLG
     EDPWVRLKTI SDAMGGVSKL TALSRGRNLF GYVPYPTSVL EGFYKEAIKN GLNIMRIFDA
     LNDLDNVKES IKLINEMGGI ADGAVCYTVD PKTEAPAEKK GFFAKLFGSK KVEEPEKIFT
     DEYFVEKAKG MEAYGAKIIT LKDMAGLVNP LRAASLISKI KAAVNVPVDF HTHCTPGYGL
     ASVVMAMLHG VDIVDTNIWY FGGGSAAPAI ELVYLFAKRL GIELEVNMEA VGRIREQLKG
     VRTALADFDL HKGDFPHDFD PLKDTLPANI EALFDKAVEA AKANDEDALL DACHAIEDYF
     NFPKPNLLVK NAEVPGGMYS NMVAQLKALN ASDVLDDAMK LIPKVRRDAG LVPLVTPTSQ
     IVGSQAVSLA IDRKKGNADY TTKSNQFISL IKGEYGKTPV AITPEFREQI TGSAVERPYD
     VASYKAPENP VLKELGGCKL AENEQEYLLL QLLPTVANGF LKKRREADHK ASAPAVEEKA
     EAAAVADDAP ITGPVERAPM GGKVVEVKVK AGDKVKKGDL LLVYEAMKME NELTAEKDAV
     VKRVFVTVDD VVGTDAPLIE FEA
//
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