ID A0A024U1L4_9STRA Unreviewed; 702 AA.
AC A0A024U1L4;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Acetyl-CoA carboxylase, biotin carboxylase subunit {ECO:0000313|EMBL:ETV99482.1};
GN ORFNames=H310_08160 {ECO:0000313|EMBL:ETV99482.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV99482.1};
RN [1] {ECO:0000313|EMBL:ETV99482.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETV99482.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; KI913967; ETV99482.1; -; Genomic_DNA.
DR RefSeq; XP_008872038.1; XM_008873816.1.
DR AlphaFoldDB; A0A024U1L4; -.
DR STRING; 157072.A0A024U1L4; -.
DR EnsemblFungi; H310_08160-t26_1; H310_08160-t26_1-p1; H310_08160.
DR EnsemblProtists; ETV99482; ETV99482; H310_08160.
DR GeneID; 20085210; -.
DR VEuPathDB; FungiDB:H310_08160; -.
DR eggNOG; KOG0238; Eukaryota.
DR OrthoDB; 1129179at2759; -.
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; 3.30.700.40; -; 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; 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; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_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; 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; PS00188; BIOTIN; 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}.
FT DOMAIN 30..476
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 149..346
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 623..698
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 702 AA; 76494 MW; CB8BBE583F13234C CRC64;
MLKLGRRALT STPLVSRWSS SFTRSDGTPM FSKILIANRG EIACRVQRTA KKLGVRTVAV
YSDADANAQH VKMADEAYRL GPPPAAESYL LFDEILRVAK ASGAQAIHPG YGFLSENAEF
CKACAAAGVE FIGPPVAAIE AMGSKSASKD IMIAAGVPVT PGYHGTDQSF ERIKAESAKI
GYPVLLKAVL GGGGKGMRIV DREEDLKDNM EACVREAKAS FASTDILVEK YLRRPRHVEL
QIFGDKHGNV VHLFERDCSV QRRHQKVLEE APAPHMSEAL RKKMGDAAVA AAKAVGYVGA
GTVEFLLDED ESFYFMEMNT RLQVEHPVTE FITQQDLVEL QLKVAAGQAL PVRQEDLKIH
GHAIEARIYA ENPYNNFLPG SGTLHHLRLP PLSDKVRVDT GIVQGDAVSI FYDPMIAKLV
VHASNRKEAI EGLMRALGQY QIVGLPTNIE FVARTAAHPE FMKGGVDTSF LLKHGDDLLT
PFSNLPSHAP ILTAVWLVLK QQHQTQRFEA TVADAGSPWT SLQNFRSLDT FHRHFTLLHD
DAPMDMDLAS TSTDGKSYIV NGTTVQVHSV DFTTGDFKLT VGNETFTGTA VVLKHDVHLF
CNDGTLAYEY KLRVPEPSYD SHGTSAGGAA SLVTPMPGKV IKVMAKAGDT IVADQPLLIM
EAMKMEHVLR APRDGQVAEM NCEVGDFVSD GHVLVEMAPA AK
//
