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Database: UniProt
Entry: D2QYM2_PIRSD
LinkDB: D2QYM2_PIRSD
Original site: D2QYM2_PIRSD 
ID   D2QYM2_PIRSD            Unreviewed;       435 AA.
AC   D2QYM2;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   SubName: Full=Oxidoreductase domain protein {ECO:0000313|EMBL:ADB18181.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Psta_3520 {ECO:0000313|EMBL:ADB18181.1};
OS   Pirellula staleyi (strain ATCC 27377 / DSM 6068 / ICPB 4128) (Pirella
OS   staleyi).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Pirellula.
OX   NCBI_TaxID=530564 {ECO:0000313|EMBL:ADB18181.1, ECO:0000313|Proteomes:UP000001887};
RN   [1] {ECO:0000313|EMBL:ADB18181.1, ECO:0000313|Proteomes:UP000001887}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27377 / DSM 6068 / ICPB 4128
RC   {ECO:0000313|Proteomes:UP000001887};
RX   PubMed=21304671; DOI=10.4056/sigs.51657;
RA   Clum A., Tindall B.J., Sikorski J., Ivanova N., Mavrommatis K., Lucas S.,
RA   Glavina del Rio T., Nolan M., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA   Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA   Goodwin L., Ovchinikova G., Pati A., Mikhailova N., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Pirellula staleyi type strain (ATCC 27377).";
RL   Stand. Genomic Sci. 1:308-316(2009).
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DR   EMBL; CP001848; ADB18181.1; -; Genomic_DNA.
DR   RefSeq; WP_012912443.1; NC_013720.1.
DR   AlphaFoldDB; D2QYM2; -.
DR   STRING; 530564.Psta_3520; -.
DR   KEGG; psl:Psta_3520; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_023194_24_0_0; -.
DR   OMA; LNTWFRF; -.
DR   OrthoDB; 9788246at2; -.
DR   Proteomes; UP000001887; Chromosome.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR   InterPro; IPR043906; Gfo/Idh/MocA_OxRdtase_bact_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR43818; BCDNA.GH03377; 1.
DR   PANTHER; PTHR43818:SF5; OXIDOREDUCTASE FAMILY PROTEIN; 1.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   Pfam; PF19051; GFO_IDH_MocA_C2; 2.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001887}.
FT   DOMAIN          48..170
FT                   /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01408"
FT   DOMAIN          215..283
FT                   /note="Gfo/Idh/MocA-like oxidoreductase bacterial type C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19051"
FT   DOMAIN          362..432
FT                   /note="Gfo/Idh/MocA-like oxidoreductase bacterial type C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19051"
SQ   SEQUENCE   435 AA;  48102 MW;  6BEC14C3DCCDC69D CRC64;
     MSDQTQIRRR TFLQSTLAAG AATAVASFVP ATALGRQGAT APSEKITLGV IGIGPRCTYD
     MKSILPMGDV QCVAIADVQA SRRDAGKKLV DDHYKNADCK LYRDFRELLD RKDIDAVLIA
     TGDRWHAAAS IMAAQAGKDV YSEKPCGITI ADCQKLADTM HAEKRVFQAG TQRRSVLNFQ
     KAVELAHSGK LGKLQTMHAS VYVPTLDNTW LPAEPTPARD VVDWNLWLGP SAWRPYNQQY
     VGGKWRGQWD FDSGARLLDW GAHTVDLCQW ANQADNTLPI DYEPTENSIV CRYANGVKLV
     IDFLQAPFGD RAPHYITRLG TCPVRFIGDE GSVETGDEGE IVASSSTLQK QLDGTKRVRG
     LDVSTHARDF FDCMRSREKT AANPDVMRRS HIACHAAAIA WILKRKLTID PVTETFVSDP
     EANLLRSRPA REWAV
//
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