ID E6ZVX1_SPORE Unreviewed; 1146 AA.
AC E6ZVX1;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=Related to PYC2-pyruvate carboxylase 2 {ECO:0000313|EMBL:CBQ71278.1};
GN ORFNames=sr16623 {ECO:0000313|EMBL:CBQ71278.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ71278.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ71278.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; FQ311443; CBQ71278.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZVX1; -.
DR EnsemblFungi; CBQ71278; CBQ71278; sr16623.
DR VEuPathDB; FungiDB:sr16623; -.
DR eggNOG; KOG0369; Eukaryota.
DR eggNOG; KOG0540; Eukaryota.
DR HOGENOM; CLU_009218_0_0_1; -.
DR OrthoDB; 1473822at2759; -.
DR Proteomes; UP000008867; Chromosome 21.
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; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
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; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR48095:SF2; BIOTIN CARBOXYLASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
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; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50989; COA_CT_CTER; 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}; Pyruvate {ECO:0000313|EMBL:CBQ71278.1}.
FT DOMAIN 2..472
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 123..329
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 508..587
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 877..1144
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 1146 AA; 121439 MW; AC5EF45886AAB530 CRC64;
MQPKRILIAN RGEIACRLMR TYRLSALPSI ETVAVYTASE SNALHVSLAD HTHALAGDGP
RAYLDRRAIV DAALKWGCWG VAPGYGFLSE DAEFARMCEG AGLVFLGPTS AQLGRLGDKV
AARELARGLK VPVVDGTSSS AASALEDILA FARDVGAGST IVLKAANGGG GRGIRILPIP
ASPADAEQAV REAYASCTRE AHAAFGDATV YAERFLSNAK HVEVQVLGDG HGGVCHFWDR
ECSLQRRNQK LVEIAPAPHL PDSLRHAMLD AALKIARAVQ LRSLATIEFL VDGPRFFFME
ANPRIQVEHT VMEAVTRVDL VALQLRVSLG HTLSDLGITS PAAAVVPTQT AIQVRINAES
FRGNTDETLP ESGTLSSVTW PLGANVRIET AAHAPHPVLG GYAVNTLFDS LLAKVVVTAA
RYGAAVDAAR RALDETAIVG VRTNVAFLKA LLSDPAVKAG QQHIHTVQAG FKGFLDVANR
LQAEIDAKQK HSTATADRTL AKKEKVEQWT EEQGKHAIRS HLSGMLVKVC VEEGQRVAEG
QELAVIEAMK MEHVIRADAD SAGGLVHRVS AQKGGIVNVS DVLLVIDTSS TPPHSHTTPT
PAAPHAAEDP AIARPELQEL QHRRHALTDA GRAAAVSKRH ARGFRTVREN LTALLDPDSL
IEYGDLTLAA QTTRYTPTDL IAKTSGDGLV AGFGRIDGHA TALLLGDYMV LAGTQGYFHH
LKLDRLLGAV LAHPAPLVLY AEGGGGRPGD TDFPVASGLQ TPSFALMGQV RASGVPVVGV
ANGYVFAGNA ALLGMCDVVV ATRGGSAGRT SIGMGGKAMI EAGGLGVVES DDIGPTHVHA
QTGGVDIVVD DEDAAALVVR QIVGFFTQPQ LDAPRWTYTH DARQLRTCLP PVHERRRAFD
MRRVIALLVD DGSFVELAPH WAPGMIAGLA RIHGHAIGVL ANDPTSPLGG AIDINAALKA
TRLLKLLTRT RAAHLLSLCD TPGFMVGPEF ERSARGGGSF RTFGDWFTAA AEFTQSGGRV
VGLVLRRAFG LGAQAMLGGS TLSNSICAAW PAGSLGSMSL EGAVQLSMKK QLAGIADETE
RARVAADAVE QLYKRGRAIN VASVAEIDTV LDPAETRDWL AKVVRDVPGV RKAVFKVNRE
RMDSRL
//
