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Database: UniProt
Entry: A0A136A2D7_9ALTE
LinkDB: A0A136A2D7_9ALTE
Original site: A0A136A2D7_9ALTE 
ID   A0A136A2D7_9ALTE        Unreviewed;      1369 AA.
AC   A0A136A2D7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Dehydrogenase {ECO:0000313|EMBL:KXI29391.1};
GN   ORFNames=AX660_14755 {ECO:0000313|EMBL:KXI29391.1};
OS   Paraglaciecola hydrolytica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Paraglaciecola.
OX   NCBI_TaxID=1799789 {ECO:0000313|EMBL:KXI29391.1, ECO:0000313|Proteomes:UP000070299};
RN   [1] {ECO:0000313|EMBL:KXI29391.1, ECO:0000313|Proteomes:UP000070299}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S66 {ECO:0000313|EMBL:KXI29391.1,
RC   ECO:0000313|Proteomes:UP000070299};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXI29391.1}.
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DR   EMBL; LSNE01000005; KXI29391.1; -; Genomic_DNA.
DR   RefSeq; WP_068376779.1; NZ_LSNE01000005.1.
DR   STRING; 1799789.AX660_14755; -.
DR   OrthoDB; 174301at2; -.
DR   Proteomes; UP000070299; Unassembled WGS sequence.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01834; SGNH_hydrolase_like_2; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR013428; Membrane-bound_put_N.
DR   InterPro; IPR013830; SGNH_hydro.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   NCBIfam; TIGR02604; Piru_Ver_Nterm; 1.
DR   PANTHER; PTHR33546; LARGE, MULTIFUNCTIONAL SECRETED PROTEIN-RELATED; 1.
DR   PANTHER; PTHR33546:SF1; LARGE, MULTIFUNCTIONAL SECRETED PROTEIN-RELATED; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   Pfam; PF13646; HEAT_2; 1.
DR   Pfam; PF13472; Lipase_GDSL_2; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   SUPFAM; SSF52266; SGNH hydrolase; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   4: Predicted;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00433}; Reference proteome {ECO:0000313|Proteomes:UP000070299}.
FT   DOMAIN          1234..1329
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
SQ   SEQUENCE   1369 AA;  153352 MW;  3DF905FBD3545BFF CRC64;
     MIFRYLVLFA LLLPVLALAK GLDHLVFEPP ANIAKGKSVV LISGDEEYRS EESLPMLAKI
     LSQRHGFKTT VLFAIDKQSG VINPNENSNI ARLDLLKNAD LMILATRWRV LPPQQLQHFL
     DYFNAAKPII ALRTATHAFN NTDHYGGYDW QNFGVNVVGE NWLNHHGEHK VQGGRGVIVE
     KNAQHPLLNN VSDIFTWSDI YGIKHLDQAK ATVLLNGAVT ESLEMDSKII DGKLNNPMMP
     LAWLKSYTTP TGDKTGPVFA TTAGAAVDFK KEDLRRLVVN ATYHLLNLKV PQKADVAFVD
     PFEPSFYGFQ EADYYLKRGL KVEDFVLGKS GKAILTKAEL ANLNVSSAIT LNKGDRIALI
     GNGLPERMLH YGHFETELLL RNPDKDLTIR TLARPGYTPG FRPHSSRNSQ WAFPGAAQFN
     PQFNHHSGEG HHPTSDEWLY DIAPDVIVAF FGFNESFAGK EGAENYRAEL SAFVDHTLAK
     QYNGKNAAKL VLVSPIAFQD LSATLDLPDG KQTNKNLALY RDIMQQVAAA KGVHFVDIFE
     PSATIFASSK TPLTVNGAHL NQAGYRLLAP ILVNGIFGQQ QLVAQAKHDE VQKLVIDKNW
     YWFQTYQMPN GVHVDGRRFE PYGVDNYPEE GKKVKQLTQN RDKALWALLS GNTFDLTAAD
     QQTQQLTPIK SNVAEEAVGE YLYGEDALAK FEMAKGYKIE LFASEVEFPN LANPAQISFD
     NQGRLWVSTL GSYPHYRPGD ARPDDKILIY EDSDGDGKAD KETVFASGLN LPIGFEITEF
     GVYVSQAPNL VLLKDTDGDD KADTYDIILS GFDTHDTHHA ISAFTADPFG NIILDEGVFL
     HSNIETAYGP VRGVNGGFYR FEPRTQKLER MVQTHIPNPW GVTYDKWGQG FFLFTSGPEV
     NWMTPVEMKT RYGQLTLGTD TLIEEAHRVR PTSGIEFISS RHFPDEVQGN LLLNNVIGFL
     GAKQHQLEDA GTGYVSHWRH DLYTSSDPNF RPVDMEFAQD GSLYVVDWHN QLIGHMQHNA
     RDPLRDHAHG RIYRVTYPER ALLAKVTITG ASPAELFELL KSPEDRIRYR AKRELRALPA
     DKLIAAKKKW LKSLDNKSTH YERYVLEAMW ASNSPNDFDQ SLVRQLLKAK DFHVRAAAVR
     ALRYQLADFE DAIPLLKKAA NDEEGRVRLE VIAAASWLDS AATINILQEV GKHPIDSWMR
     NAFLQTMNNV GGTWEFKEEV VANEAAHLPE VLQQTYFKGK DIYRKEGYCS TCHQVDGFGL
     PAAQFPPLAG TDWVTGNPER LIDIALYGIM GKVWVKNVEY VGHVPMTPFQ GLLNDEEMAA
     VLTYVRNAFG NKASAISPEQ VKNVRDGGQE PQGFWTAEAL KKKYPDAEY
//
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