ID A6RAJ1_AJECN Unreviewed; 674 AA.
AC A6RAJ1;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 24-JAN-2024, entry version 83.
DE RecName: Full=Pyruvate carboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HCAG_05979 {ECO:0000313|EMBL:EDN10176.1};
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN10176.1, ECO:0000313|Proteomes:UP000009297};
RN [1] {ECO:0000313|Proteomes:UP000009297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CH476661; EDN10176.1; -; Genomic_DNA.
DR AlphaFoldDB; A6RAJ1; -.
DR STRING; 339724.A6RAJ1; -.
DR VEuPathDB; FungiDB:HCAG_05979; -.
DR HOGENOM; CLU_000395_3_2_1; -.
DR OMA; KGDAWSI; -.
DR OrthoDB; 2785982at2759; -.
DR Proteomes; UP000009297; 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 CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
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; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR45007; CARBOXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G07570)-RELATED; 1.
DR PANTHER; PTHR45007:SF1; CARBOXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G07570)-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 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 SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000009297}.
FT DOMAIN 8..458
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 126..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 578..659
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 569..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 674 AA; 73611 MW; 983215F569226622 CRC64;
MSLPPARPIK RLLVANRGEI AIRILQAARE LPNIETFALY TADDRSHCDL GAPHHAVSLP
SPSSYMDIAL LVQLAREHSI DAIHPGYGFL SESAEFAQRM WEEAGVKVIG PGWEVLARTG
DKLQAKMLAE ACRVPILKAM RTPTSDIGLI RQFVAEVGYP VMVKAVDGGG GRGIRFVKGP
DELQSAIDRA TGESPSKKVF VEKAAVGGFH HIEVQVVGDG TGEVRHLWER DCSVQRRFQK
IVECAPAMMK NRTLIKRVIE SALRMASEIK YLSLGTFEFL ASEKLSKFYF LEINPRLQVE
HTITECISTV DLVQTQLLLA QGVSLRDMGL GDIKNPEQPP ATYSIQLRLC AEDPTADFAL
SIGKITEFHV PGGNGVRVDT HISGSSSLVI GSDFDNMMAK IIVTSTSWDG VVRKACRVLN
DARISGVKTN IDVLKGIIGN IEFQEWQIDT QWMEKNLGDI IQHGKQLSSS NLNRSSLPSL
PSFSASQALS FGSSSVLFRK GDAWSVELAP LNSTKGPGSQ APHHHLLLSK LLRNEFPTSL
SAEIEYTTPA TATQTATITP YRVTLARTSA SSSSLSSTHR RGNPNNSSHI TLPMSGKVTE
MLVEEGDEIQ ENTVIAFVKQ MKMELEVRSP KAGRVTWALE LEDGNGEDVP EGILLAEITP
IDPPEQGVEV KGKL
//
