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Database: UniProt
Entry: F5YN74_TREPZ
LinkDB: F5YN74_TREPZ
Original site: F5YN74_TREPZ 
ID   F5YN74_TREPZ            Unreviewed;       401 AA.
AC   F5YN74;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Aldo/keto reductase {ECO:0000313|EMBL:AEF84990.1};
GN   OrderedLocusNames=TREPR_0302 {ECO:0000313|EMBL:AEF84990.1};
OS   Treponema primitia (strain ATCC BAA-887 / DSM 12427 / ZAS-2).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC   Treponema.
OX   NCBI_TaxID=545694 {ECO:0000313|EMBL:AEF84990.1, ECO:0000313|Proteomes:UP000009223};
RN   [1] {ECO:0000313|Proteomes:UP000009223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC   {ECO:0000313|Proteomes:UP000009223};
RA   Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A.,
RA   Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X., Lucey K.,
RA   Ballor N.R., Ottesen E., Rosenthal R., Allen A., Leadbetter J.R.,
RA   Paulsen I.T.;
RT   "Complete sequence of Treponema primitia strain ZAS-2.";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEF84990.1, ECO:0000313|Proteomes:UP000009223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC   {ECO:0000313|Proteomes:UP000009223};
RX   PubMed=21326336; DOI=10.1038/ismej.2011.3;
RA   Rosenthal A.Z., Matson E.G., Eldar A., Leadbetter J.R.;
RT   "RNA-seq reveals cooperative metabolic interactions between two termite-gut
RT   spirochete species in co-culture.";
RL   ISME J. 5:1133-1142(2011).
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DR   EMBL; CP001843; AEF84990.1; -; Genomic_DNA.
DR   RefSeq; WP_015709693.1; NC_015578.1.
DR   AlphaFoldDB; F5YN74; -.
DR   STRING; 545694.TREPR_0302; -.
DR   KEGG; tpi:TREPR_0302; -.
DR   eggNOG; COG1453; Bacteria.
DR   HOGENOM; CLU_023205_3_2_12; -.
DR   OrthoDB; 9773828at2; -.
DR   Proteomes; UP000009223; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd19096; AKR_Fe-S_oxidoreductase; 1.
DR   Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   PANTHER; PTHR43312; D-THREO-ALDOSE 1-DEHYDROGENASE; 1.
DR   PANTHER; PTHR43312:SF2; OXIDOREDUCTASE-RELATED; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   Pfam; PF13187; Fer4_9; 1.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000009223}.
FT   DOMAIN          16..266
FT                   /note="NADP-dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00248"
FT   DOMAIN          295..363
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|Pfam:PF13187"
SQ   SEQUENCE   401 AA;  45623 MW;  EC35580413070C1C CRC64;
     MQYRLDKKTG NKLSVLGFGS LRFPKKFGTT DLQKTEPLVM RAIEGGVNYF DAGYFYFGSE
     EVLGTIFERN KIREKVHFAT KMPLVLVRGP EDFDKFFNKQ LERIRSNYID YYLIHMLPDI
     ESWKNLCKWG IEDWIREKKR QGAIRSMGFS FHGRQNEFLS LIDAYDWDFC QIQYNYSDEN
     FQAGVTGLKK ASAKGMPVMI MEPLLGGKLV GGLSPKAVDI FKQANPDWSP AGWGFRWLWN
     QKEVTVTLSG MTDISQIEEN LKAADTAAPG LLSQADMEVY GRVQEEFKSA YKVLCTGCNY
     CMPCPQQVNI PACFAAYNIS YTMGRLTGIQ NYIFSNVLVD SKEFGGAGLC IKCGACEKKC
     SQNIPIIKTL QAVRKRLEPP WVKWPMLFFG GLFKKFGGRK A
//
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