ID   PLH35_FORAG             Reviewed;         321 AA.
AC   T2KNC8;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2013, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Oxidoreductase P35 {ECO:0000305};
DE            EC=1.-.-.- {ECO:0000305};
DE   AltName: Full=P35_oxidoreductase {ECO:0000303|PubMed:31285597};
DE   AltName: Full=Polysaccharide utilization locus H protein P35 {ECO:0000303|PubMed:31285597};
DE            Short=PUL H protein P35;
GN   ORFNames=BN863_22240;
OS   Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 /
OS   M-2Alg 35-1).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Formosa.
OX   NCBI_TaxID=1347342;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1;
RX   PubMed=23995932; DOI=10.1128/aem.01937-13;
RA   Mann A.J., Hahnke R.L., Huang S., Werner J., Xing P., Barbeyron T.,
RA   Huettel B., Stueber K., Reinhardt R., Harder J., Gloeckner F.O.,
RA   Amann R.I., Teeling H.;
RT   "The genome of the alga-associated marine flavobacterium Formosa agariphila
RT   KMM 3901T reveals a broad potential for degradation of algal
RT   polysaccharides.";
RL   Appl. Environ. Microbiol. 79:6813-6822(2013).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=31285597; DOI=10.1038/s41589-019-0311-9;
RA   Reisky L., Prechoux A., Zuehlke M.K., Baeumgen M., Robb C.S., Gerlach N.,
RA   Roret T., Stanetty C., Larocque R., Michel G., Song T., Markert S.,
RA   Unfried F., Mihovilovic M.D., Trautwein-Schult A., Becher D., Schweder T.,
RA   Bornscheuer U.T., Hehemann J.H.;
RT   "A marine bacterial enzymatic cascade degrades the algal polysaccharide
RT   ulvan.";
RL   Nat. Chem. Biol. 15:803-812(2019).
CC   -!- FUNCTION: Oxidoreductase that may be involved in ulvan degradation
CC       (Probable). Ulvan is the main polysaccharide component of the Ulvales
CC       (green seaweed) cell wall. It is composed of disaccharide building
CC       blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic
CC       acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl) (Probable).
CC       {ECO:0000305|PubMed:31285597}.
CC   -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000305|PubMed:31285597}.
CC   -!- INDUCTION: By ulvan. {ECO:0000269|PubMed:31285597}.
CC   -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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DR   EMBL; HG315671; CDF79936.1; -; Genomic_DNA.
DR   RefSeq; WP_038530545.1; NZ_HG315671.1.
DR   AlphaFoldDB; T2KNC8; -.
DR   SMR; T2KNC8; -.
DR   STRING; 1347342.BN863_22240; -.
DR   EnsemblBacteria; CDF79936; CDF79936; BN863_22240.
DR   PATRIC; fig|1347342.6.peg.2231; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_023194_1_3_10; -.
DR   OMA; CHILDRI; -.
DR   OrthoDB; 1465613at2; -.
DR   Proteomes; UP000016160; Chromosome.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR   InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   Pfam; PF02894; GFO_IDH_MocA_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..321
FT                   /note="Oxidoreductase P35"
FT                   /id="PRO_0000448298"
SQ   SEQUENCE   321 AA;  35981 MW;  18944CBBF2307053 CRC64;
     MESRINWGII GCGNVAEVKS GPAFYKTENS TLVAVMRRNE DKVIDFANRH GVANWTTNAE
     ALIQNDLINA VYIATPPSSH LQYALRAINV GKNVYLEKPM VLNNHEANIL VEAVKRSNVK
     VTVAHYRREL PVYLKIKELL DSNVIGNVIS AEIQIKQTRN TNLIAKTEVN WRTIPEISGG
     GYFHDIAPHQ IDLMCHYFGE VENIKKGSCK ENQVSHQDVS GEVLFKNGVQ FSGTWNFNAL
     EDKDECTIKG ERGSISFSFY TSTITVSKNG LIESYHYENP EHVQQPMIEK TVGYFLAHNS
     NPCSVEEAAM VTHIMDVFCG T