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Database: UniProt
Entry: C1G9C3_PARBD
LinkDB: C1G9C3_PARBD
Original site: C1G9C3_PARBD 
ID   C1G9C3_PARBD            Unreviewed;       333 AA.
AC   C1G9C3;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 2.
DT   24-JAN-2024, entry version 68.
DE   SubName: Full=Chlorophyll synthesis pathway protein BchC {ECO:0000313|EMBL:EEH47775.2};
GN   ORFNames=PADG_03859 {ECO:0000313|EMBL:EEH47775.2};
OS   Paracoccidioides brasiliensis (strain Pb18).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH47775.2, ECO:0000313|Proteomes:UP000001628};
RN   [1] {ECO:0000313|EMBL:EEH47775.2, ECO:0000313|Proteomes:UP000001628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pb18 {ECO:0000313|EMBL:EEH47775.2,
RC   ECO:0000313|Proteomes:UP000001628};
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; KN275960; EEH47775.2; -; Genomic_DNA.
DR   RefSeq; XP_010759214.1; XM_010760912.1.
DR   AlphaFoldDB; C1G9C3; -.
DR   STRING; 502780.C1G9C3; -.
DR   GeneID; 22583095; -.
DR   KEGG; pbn:PADG_03859; -.
DR   VEuPathDB; FungiDB:PADG_03859; -.
DR   eggNOG; KOG0024; Eukaryota.
DR   HOGENOM; CLU_026673_11_0_1; -.
DR   InParanoid; C1G9C3; -.
DR   OMA; FETWYAM; -.
DR   OrthoDB; 2084524at2759; -.
DR   Proteomes; UP000001628; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08234; threonine_DH_like; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR   PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001628};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          21..123
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          162..293
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   333 AA;  35729 MW;  E0BEB4F3D83D3802 CRC64;
     MPPDTPSPRS LDLSTSPSQR CIKVKACGVC GTDLHIHEGE FLAKFPLVPG HETVGEVAAL
     GPKVKGFTIG DRVVADNSEL CGTCFYCRRG EELLCENFEA HGVTMNGGFA EYCAYPAGRV
     FKIQNLSDAD ATLLEPASCA AHGLDKISPK MGSTVLMFGA GPTGLVLAQM LKLNGGCKVV
     IAAPEGLKMD LAKSLNAGDE YISLSRKDPS AQFAKLKADN PYGFDIVVEA TGSVKILEDA
     INYVRRGGKL VVYGVYAAKD RVTWPPSKIF GDEITILGSF SETYKFPAAI DYLDSGKVKV
     NGIVNKVFKI EQWAECLESM RNKSAIKAAI VFD
//
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