ID A6LCC1_PARD8 Unreviewed; 705 AA.
AC A6LCC1;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 84.
DE SubName: Full=Putative zinc-binding dehydrogenase {ECO:0000313|EMBL:ABR43335.1};
GN OrderedLocusNames=BDI_1580 {ECO:0000313|EMBL:ABR43335.1};
OS Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS 5825 / NCTC 11152).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=435591 {ECO:0000313|EMBL:ABR43335.1, ECO:0000313|Proteomes:UP000000566};
RN [1] {ECO:0000313|EMBL:ABR43335.1, ECO:0000313|Proteomes:UP000000566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152
RC {ECO:0000313|Proteomes:UP000000566};
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(2007).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; CP000140; ABR43335.1; -; Genomic_DNA.
DR RefSeq; WP_011966515.1; NC_009615.1.
DR AlphaFoldDB; A6LCC1; -.
DR STRING; 435591.BDI_1580; -.
DR PaxDb; 435591-BDI_1580; -.
DR KEGG; pdi:BDI_1580; -.
DR PATRIC; fig|435591.13.peg.1567; -.
DR eggNOG; COG0673; Bacteria.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_024115_0_0_10; -.
DR OMA; YVRWTER; -.
DR BioCyc; PDIS435591:G1G5A-1624-MONOMER; -.
DR Proteomes; UP000000566; Chromosome.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR CDD; cd08255; 2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_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; 2.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43350:SF19; D-GULOSIDE 3-DEHYDROGENASE; 1.
DR PANTHER; PTHR43350; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR Pfam; PF02894; GFO_IDH_MocA_C; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000566}.
FT DOMAIN 178..297
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
FT DOMAIN 389..497
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT DOMAIN 544..618
FT /note="Gfo/Idh/MocA-like oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02894"
SQ SEQUENCE 705 AA; 76980 MW; 57BD2A079F4B3BA4 CRC64;
MKQIIQDLKS GSTILEEVPV PQVKSGYVLI QTTRTLVSLG TERMLVEFGK ANLIDKARQQ
PDKVKQVLDK IKTDGLQPTL EAVFNKLGQP LPLGYCNVGR VVAVGKGVAE FKVGDRVASN
GNHAEFVCVP KNLVAKVPDD ITDEEAAFTV IGSIGLQGIR LLNPQLGETV VVVGLGLIGL
VAAQLLRANG CKVIGVDFDQ QKVDMAASKG IVAVNPGRGT DPVRFVEDYT GGIGADGVLI
TASTQNHEVI HQASEMSRKR GRIVLVGVVG LNMRRDDFYK KELSFQVSCS YGAGRYDEEY
ENKGHDYPLA YVRWTEKRNF ETILHAISSG SLDVKSLITE EVDLADYEEI YGDMRKKGSI
ASILRFPADS KMESVVSIGS NAFVSGNGKI GIIGAGNYTS AMIIPCLAKA HARIKYIASA
QGLSAKILAR KAGAENATSD YQNILKDPEV DLVMVTTRHN LHARMVIEAL RNGKSVFVEK
PLCLNETELD DIIRAYQGAP EGTTLTVGFN RRFSPFAEKM RRLLGDGPKN IVATMNAGFI
PREVWVHDLE IGGGRIIGEA CHFIDLCSFL AGSEVVAVCM NALGENPEEN TDNASILLRY
ANGTNAVINY FANGSKSYAK ERVEVFSQER VLVLDNWRKL TGYGFKGFSS MKAGMDKGQK
RQFTLLNERI REGGEPLIPF ESILNTTKAT FACITSLKER CWVNL
//