ID A0A1G0J7H2_9GAMM Unreviewed; 690 AA.
AC A0A1G0J7H2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Cytochrome c domain-containing protein {ECO:0000259|PROSITE:PS51007};
GN ORFNames=A3H44_01135 {ECO:0000313|EMBL:OGT70350.1};
OS Gammaproteobacteria bacterium RIFCSPLOWO2_02_FULL_57_10.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1798299 {ECO:0000313|EMBL:OGT70350.1, ECO:0000313|Proteomes:UP000178443};
RN [1] {ECO:0000313|EMBL:OGT70350.1, ECO:0000313|Proteomes:UP000178443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- COFACTOR:
CC Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC Evidence={ECO:0000256|ARBA:ARBA00001931};
CC -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008156}.
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:OGT70350.1}.
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DR EMBL; MGYS01000090; OGT70350.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0J7H2; -.
DR STRING; 1798299.A3H44_01135; -.
DR Proteomes; UP000178443; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR Gene3D; 2.140.10.10; Quinoprotein alcohol dehydrogenase-like superfamily; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR PANTHER; PTHR32303; QUINOPROTEIN ALCOHOL DEHYDROGENASE (CYTOCHROME C); 1.
DR PANTHER; PTHR32303:SF20; QUINOPROTEIN ETHANOL DEHYDROGENASE; 1.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR Pfam; PF01011; PQQ; 1.
DR Pfam; PF13360; PQQ_2; 1.
DR SMART; SM00564; PQQ; 5.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 3: Inferred from homology;
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}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 28..107
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 690 AA; 74110 MW; CF42607531D0967D CRC64;
MLIAGYAAQA EAQQGAQAGA PTGIYTAQQA SAGAVEYQTN CAACHGAQLQ GTTAAPLLAG
TPFLSRWGTR GAGDLFGYIK SSMPPGSTTP LADDTVGNVV AYMLQVNGAV AGAQPVGAAT
TAAIASGIPA TAAPVAQQQR QEEELLGVTF AGTVDEYTPI TTEIMENPDP SDWLMFRGNH
HAWSYSELDQ INRGNVDDLQ LEWVWTMHEG ASEPAPLVYD GIMFLINTSN IIQALDAATG
ELIWEHRAGP ATREDMRNIA LYGDKVFHAT TDARLLALDA RTGEKVWEVV VADSSKGFAN
SSGPIVADGK VILGMAGCAR YINENCYMTA HDPETGERLW EFNTVAHADT PGGDTWGGLD
NMFRKGGETW IAGSYDPATR LTYWGTAQAK PWVPVSRHMS IHDAGLYTNA TIALDIDSGQ
LAWHFQHVPG EALDLDEVFE RILVDRDGQQ LVFSLGKHGI LWKNDRVTGQ FLGFKETMFQ
NTFTHIDPVT GAVTYRDDII NAQLDEWTSA CPSSAGGKDW HSMSYHEPSG VLIAPLSQTC
LENAARAVEL VEGSGGTAAS RRFFEMPGTD GNVGKLAAYD VSTMEEVWSY EQRASFLTGV
ISTAGGVAFA GDLDRRFRAF DVRTGEILWE TRLGTSVQGH PLTFSVDGKQ YVAVTAAVGG
TSPRMVPAVV TPEITYPNNG NAIYVFSLKD
//
