ID   A0A1G4JM08_9SACH        Unreviewed;      1828 AA.
AC   A0A1G4JM08;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   13-SEP-2023, entry version 23.
DE   SubName: Full=LAMI_0E06722g1_1 {ECO:0000313|EMBL:SCU91648.1};
GN   ORFNames=LAMI_0E06722G {ECO:0000313|EMBL:SCU91648.1};
OS   Lachancea mirantina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1230905 {ECO:0000313|EMBL:SCU91648.1, ECO:0000313|Proteomes:UP000191024};
RN   [1] {ECO:0000313|EMBL:SCU91648.1, ECO:0000313|Proteomes:UP000191024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 11717 {ECO:0000313|EMBL:SCU91648.1};
RA   Devillers H.;
RL   Submitted (MAR-2016) 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; LT598465; SCU91648.1; -; Genomic_DNA.
DR   STRING; 1230905.A0A1G4JM08; -.
DR   OrthoDB; 313213at2759; -.
DR   Proteomes; UP000191024; Chromosome e.
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   GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 1.20.58.1700; -; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.1360.40; -; 1.
DR   Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 2.
DR   Gene3D; 3.10.490.10; Gamma-glutamyl cyclotransferase-like; 1.
DR   InterPro; IPR014085; Allophanate_hydrolase.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
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; 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   InterPro; IPR014084; Urea_COase.
DR   NCBIfam; TIGR02713; allophanate_hyd; 1.
DR   NCBIfam; TIGR00724; urea_amlyse_rel; 1.
DR   NCBIfam; TIGR02712; urea_carbox; 1.
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; PF01425; Amidase; 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; SSF75304; Amidase signature (AS) enzymes; 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; PS00188; BIOTIN; 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:UP000191024}.
FT   DOMAIN          624..1067
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          743..940
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1750..1828
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   1828 AA;  201642 MW;  C6DB33F38F0AC0E9 CRC64;
     MSTDTYGWTV QDWLRFHADS TPEVSFKALL ALVKSQKQAP EDPAWISVAS EGNLDQQWKI
     LQSKAHKDTL PLYGVPVAIK DNIDARGFDT TAACPSFRYT PAQDSTVVAL LRDAGAIIVG
     KTNLDQFATG LVGTRSPYGK TPCVFSDKHV SGGSSAGSSS VVGRGIVPLA LGTDTAGSGR
     VPAALNNLIG LKPTRGIFSC YGVVPACKSL DCVSVFAFNL KDAETCLKVM AKPDSEKDEY
     SRPLPANPLR KYPQHVKVAI PKQLYWYGET HNPKIYEDAV ENLKKTGAEV SVLDFEPLLD
     LARCLYEGAW VAERYEATRD FFATNPPKST LDPTVTAIIK SATKFDAADA FKFEYKRQGI
     LQKVKKALKE VDVLCVPTCP LNPTFEQIEA EPVLVNSRQG TWTNFVNLAD MAALAIPAGF
     RPDGLPNGVT LIGKKFTDFA LLDLANRFFK EAFPNNSRSY GVFTDKQVNL EDELEGPEGC
     LKNSIRLAVV GAHLKGLPLH WQLEAVNAQY LASPKTSKNY KLYALPKTGP VLKPGLRRVE
     STTGSQIQLE VYSVPKDKFG TFITMVPEPL GIGSVELESG EWVKSFICEE FGYTQKGTVD
     ITSYGSFKTY VEYLEREDAK TKKPFQTVLI ANRGEIAVRI IKTLKKLGIK SVAVYSDPDK
     YSRHVTDADF AVPLHGRTAA ETYLDIDKII TAAKETNSEA IIPGYGFLSE NADFSDRCGQ
     EGIVFVGPSG DAIRKLGLKH SAREIAAKAG VPLVPGSGLI SSPQEAKKVA REIEYPVMVK
     STAGGGGIGL QKVDSEDEIE RVFETVQHQG KAYFGDSGVF LERFVENARH VEIQMMGDGR
     GKAIAIGERD CSLQRRNQKV IEETPAPNLS EKTRLRMRKA SENLGSLLNY KCAGTVEFIY
     DEKRDEFYFL EVNARLQVEH PITEMTTGLD LVEWMLRIAA DDPPDFDSTK IGVNGASIEA
     RLYAENPIKD FRPSPGQLTD VKFPGWARVD TWVEKGTVVS AEYDPTLAKI IVHGKDRNDA
     IIKLNKALEE TVIYGCVTNI DYLRSIASSD MFKSAKVATK VLDSFDYKAN AIEVLAPGAY
     TTVQDYPGRK GYWRIGVPPS GPMDAYSFRL ANRIVGNHEK APAIEITLNG PKILFHHECD
     IAISGGVAPC TINDQPVDLN KPITVKRGDT LAIGKLVSGC RSYLAVRGGI DVPEYLGSRS
     TFALGNMGGY NGRVLKLGDV LFINKPELAS TNIPAPMYEP AMAPNSLIPQ IAQKEWQIGV
     TCGPHGSPDF FKPESIEEFF AEKWKVHYNS NRFGVRLVGP KPKWARNDGG EGGLHPSNAH
     DYVYSLGAIN FTGDEPVIIT SDGPSLGGFV CQAVVPEAEL WKVGQVKPGD LIQFVPVSYE
     TARCLKESQD NAIASFQDGS LKVLNEKLVL PKYEDPILAQ LAKRSDLSPK VTYRQAGDRY
     VLVEYGENEM DLNISYRVNR LISTVEKHHT VGIIEMSQGV RSVLIEFDGY LISQKRLVDT
     LIAYEQEIHF DKNWSIKSKI LKLPLAFEDS KTLECVKRYQ ETIRSSAPWL PNNVDFIADV
     NDITHKDVED MLYSARFLVL GLGDVFLGAP CAVPLDPRHR FLGSKYNPSR TYTKNGTVGI
     GGMYMCIYAM DSPGGYQLVG RTIPIWDKLK LGTHSKEHPW LLTPFDQVEF YPVSEAELDK
     FTEDCSNGKF SVQIEEGVFD HKRYLEWIDK NIDSITKFQE SQKGSKAEEF AKLIQVSNAE
     LEQTTGSTAA PEQSYPENAE FVYSEYSGRF WKPTVTVGDK VSKGQSLVIV EAMKTEMVVA
     APREGKVLDI LHKNGDMVEA GDVVVVIE
//