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Database: UniProt
Entry: H5SCF2_9BACT
LinkDB: H5SCF2_9BACT
Original site: H5SCF2_9BACT 
ID   H5SCF2_9BACT            Unreviewed;       320 AA.
AC   H5SCF2;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:BAL53838.1};
GN   ORFNames=HGMM_F10C03C06 {ECO:0000313|EMBL:BAL53838.1};
OS   uncultured Acidobacteriota bacterium.
OC   Bacteria; Acidobacteriota; environmental samples.
OX   NCBI_TaxID=171953 {ECO:0000313|EMBL:BAL53838.1};
RN   [1] {ECO:0000313|EMBL:BAL53838.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16309394; DOI=10.1111/j.1462-2920.2005.00881.x;
RA   Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S.,
RA   Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.;
RT   "Genetic and functional properties of uncultivated thermophilic
RT   crenarchaeotes from a subsurface gold mine as revealed by analysis of
RT   genome fragments.";
RL   Environ. Microbiol. 7:1967-1984(2005).
RN   [2] {ECO:0000313|EMBL:BAL53838.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Takami H., Noguchi H., Takaki Y., Uchiyama I., Toyoda A., Nishi S.,
RA   Chee G.-J., Arai W., Nunoura T., Itoh T., Hattori M., Takai K.;
RT   "A Deeply Branching Thermophilic Bacterium with an Ancient Acetyl-CoA
RT   Pathway Dominates a Subsurface Ecosystem.";
RL   PLoS ONE 7:e30559-e30559(2012).
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DR   EMBL; AP011669; BAL53838.1; -; Genomic_DNA.
DR   AlphaFoldDB; H5SCF2; -.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43377; BILIVERDIN REDUCTASE A; 1.
DR   PANTHER; PTHR43377:SF1; BILIVERDIN REDUCTASE A; 1.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          1..110
FT                   /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01408"
SQ   SEQUENCE   320 AA;  36998 MW;  0EC78574179407DE CRC64;
     MRFLIIGCGS MGKRRIRNLL HLGETDLLAF DPREDRRQEV TARYGVSAFS TFEEALAHEP
     EALVISTPPA LHAPYVEWAI RHNVHFFCEV PLSPHPSEIE RFLHLMRESG FHRVAAPSST
     WKFLPTVRML QQLLNEPWFA PALCVLHQVG QYLPDWHPWE DYRTFYAADL KLGGGLDVPA
     IELNWMLWLL GDTRVKRVQG VARKLSRLEI HTADVLQLLM ECENGVLLSM HFDMIQRKGE
     RYVKFISENG TIVWEGWTVR FFRASGTDWT FLPELEPEAI EQTYVEEMRA FLAAIRGEAA
     FPNDLPTEHH IMTVLRQVLP
//
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