ID A0A166ZE18_METRR Unreviewed; 1240 AA.
AC A0A166ZE18;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Acetyl-/propionyl-coenzyme A carboxylase alpha chain {ECO:0000313|EMBL:OAA37823.1};
GN ORFNames=NOR_06900 {ECO:0000313|EMBL:OAA37823.1};
OS Metarhizium rileyi (strain RCEF 4871) (Nomuraea rileyi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1081105 {ECO:0000313|EMBL:OAA37823.1, ECO:0000313|Proteomes:UP000243498};
RN [1] {ECO:0000313|EMBL:OAA37823.1, ECO:0000313|Proteomes:UP000243498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 4871 {ECO:0000313|EMBL:OAA37823.1,
RC ECO:0000313|Proteomes:UP000243498};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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:OAA37823.1}.
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DR EMBL; AZHC01000028; OAA37823.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166ZE18; -.
DR STRING; 1081105.A0A166ZE18; -.
DR OMA; TLQMWNR; -.
DR OrthoDB; 313213at2759; -.
DR Proteomes; UP000243498; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 3.30.1360.40; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 2.
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; IPR003778; CT_A_B.
DR InterPro; IPR003833; CT_C_D.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
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 Pfam; PF02626; CT_A_B; 1.
DR Pfam; PF02682; CT_C_D; 1.
DR SMART; SM00796; AHS1; 1.
DR SMART; SM00797; AHS2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF160467; PH0987 N-terminal 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; 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}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000243498}.
FT DOMAIN 11..466
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 129..327
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1153..1237
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1240 AA; 134540 MW; 0F10E399BE8D16D3 CRC64;
MGNLMPPPLS NIRKVLIANR GEIAVRCIKA CRDVQVHSIS IFTNADATSL HVTLADQAEH
LPGDDGTAYA DAEAILTICK STGADAIIPG CGFLSEDADF AAAVSSAGII FVGPCPESIK
AMGLKHEARA IAEAAQVPVV PGTRLLASAA QVIEAAKSLE FPVMLKATAG GGGMGLQVCH
SEHEAQEAFS MVESRASTLF KNGGLFLEKY YERSHHIEVQ VVGNGNIVVA LGERECSLQR
RHQKVIEECP SPFVERNPGL RERLLQAASS YASQLKYKSV GTVEFLVDDE TAEFFFLEMN
TRLQVEHGIT ELCYGVDLVH LMLLQADYER AGHPGIPSDL LEDLKMNQPL GSAIEARVYA
EMPLRDFVPS PGVLQLVNWP KGEGVRVDTW VRNGQRITPL YDPLIGKILV HSSAGRVAAH
ARLRAALVET TLQGTQTNLE YLIKIVDSSI FVSGDTLTNS LSTFKFESCS LQVLDPGVFT
TIQDYPGRST VGHGVPPGGP MDDLSARAAN ILVGNDSGIE LLEVTLAGPE LLFHEAAVVA
ICGAQLPVTV GDEPQPMWSR VVVKKGQILK LGKITGHGTR AYLAVKGGFP QIPMFLGSKS
TAPELGFGGL QGRKLHSQDI IHLHQRSGHW AAAATGLSLP ANAIPDYKIT SVCCIDGPYG
CDEILTAEGR KTLYETEWVV SHNSGRSGIR LNGPRLRWAR TSGGGGGSHP SNVLDYGYPN
GGVNFTGESP IIFAHDRPDL GGFACPTTVC SAEMWKVGQL NAGTKVQFRS VSYDTALDMT
RKKNEYLGAL TAYSQGDACE IPSLDLELND EPPCSILHRA APSGTHPKVT YRQGGDTSII
IEYGEQIPDL RNTACIQLLA QALLAADFGG VRGEPNFATL TIRFDPFLLE RSKLIERLIQ
LDGEIGETTG IKIPARQVRL PVCLDHTSLR ESAQRYMESI RPNAAYLPDN VEYLRKNNAL
STRHDVFDAI LKTPWLTVAV GFYVGTPIMF PLDPWRVLTG QKYNPSRVYT PGGSIGLGGS
LAAIYPVDAP GGYQLMGRTL GGWDAGGNRP GFSSARPWLF QHFDMIQFYE VSEEEYEKME
QQFEIGRYEF DITDTTIDMD TYISRFDEAA RDPKYRAWRA RQAVASQEVG ELEQRLFEQW
AETKRAMQSG PDPGLEGDAV NSDEAVSVAS PMDATVWKVL VQQGDVLEKE QTVAVLEAMK
MEINVVVSAN QAGAVVTEIS KPPGSIVAPG TSIVRAMRPE
//
