GenomeNet

Database: UniProt
Entry: A0A2N0WWT4_9GAMM
LinkDB: A0A2N0WWT4_9GAMM
Original site: A0A2N0WWT4_9GAMM 
ID   A0A2N0WWT4_9GAMM        Unreviewed;       388 AA.
AC   A0A2N0WWT4;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Di-heme enzyme {ECO:0000313|EMBL:PKF60598.1};
GN   ORFNames=CW745_13785 {ECO:0000313|EMBL:PKF60598.1};
OS   Psychromonas sp. psych-6C06.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=2058089 {ECO:0000313|EMBL:PKF60598.1, ECO:0000313|Proteomes:UP000233619};
RN   [1] {ECO:0000313|EMBL:PKF60598.1, ECO:0000313|Proteomes:UP000233619}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=psych-6C06 {ECO:0000313|Proteomes:UP000233619};
RX   PubMed=27311813; DOI=.1038/ncomms11965;
RA   Datta M.S., Sliwerska E., Gore J., Polz M.F., Cordero O.X.;
RT   "Microbial interactions lead to rapid micro-scale successions on model
RT   marine particles.";
RL   Nat. Commun. 7:11965-11965(2016).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000294-1};
CC       Note=Binds 2 heme groups. {ECO:0000256|PIRSR:PIRSR000294-1};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC   -!- PTM: Binds 2 heme groups per subunit. {ECO:0000256|PIRSR:PIRSR000294-
CC       1}.
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:PKF60598.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; PIZM01000010; PKF60598.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N0WWT4; -.
DR   OrthoDB; 9805202at2; -.
DR   Proteomes; UP000233619; Unassembled WGS sequence.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 2.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR004852; Di-haem_cyt_c_peroxidsae.
DR   InterPro; IPR023929; Di-heme_enz_MXAN0977.
DR   InterPro; IPR026259; MauG/Cytc_peroxidase.
DR   NCBIfam; TIGR04039; MXAN_0977_Heme2; 1.
DR   PANTHER; PTHR30600:SF12; BLL6722 PROTEIN; 1.
DR   PANTHER; PTHR30600; CYTOCHROME C PEROXIDASE-RELATED; 1.
DR   Pfam; PF03150; CCP_MauG; 1.
DR   PIRSF; PIRSF000294; Cytochrome-c_peroxidase; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 2.
DR   PROSITE; PS51007; CYTC; 1.
PE   4: Predicted;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000294-1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000294-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000294-2};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233619};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..388
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014754711"
FT   DOMAIN          215..367
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   BINDING         83
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT   BINDING         86
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT   BINDING         87
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000294-2"
FT   BINDING         231
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT   BINDING         234
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT   BINDING         235
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000294-2"
SQ   SEQUENCE   388 AA;  43133 MW;  2C1B8333D16C164B CRC64;
     MSAQYKICLL ILSAGFYLAG CDSESHYEVA PVSSTNDQGF DYLNGAFPEP HEPEDNKATE
     AKFQLGRHLF YDKRLSGNQT QSCESCHFQS LAFTDGKVQS IGSTGDLLSR NASTLTNVGY
     NATYTWSNPV LKHIESQLVI PMFGEFPVEL GINDGNKEAI LSRFKDDNEY VQRFNLAFPN
     QDAPISLPNI IKSLAVFNRA LISNDSDFDR GEMSSSAMRG QALFNSEKME CFHCHSGFNF
     TDSTLHEDTV FVSRPFFNTG LYNLDEEGSY PAIDNGLFEV TQQPGDKGKF RPPTLRNITL
     TAPYMHDGSI ATLDEVLAFY AQGGRNIIEG EFIGDGRNNP NKSEFVNGFS LSEQEKADLI
     AFLTALTDHA FVANPRFNNP FLNEVNND
//
DBGET integrated database retrieval system