ID A0A0S9C870_9SPHN Unreviewed; 761 AA.
AC A0A0S9C870;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Cytochrome c domain-containing protein {ECO:0000259|PROSITE:PS51007};
GN ORFNames=ASE95_16815 {ECO:0000313|EMBL:KQN89831.1};
OS Sphingomonas sp. Leaf231.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736301 {ECO:0000313|EMBL:KQN89831.1, ECO:0000313|Proteomes:UP000051427};
RN [1] {ECO:0000313|EMBL:KQN89831.1, ECO:0000313|Proteomes:UP000051427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf231 {ECO:0000313|EMBL:KQN89831.1,
RC ECO:0000313|Proteomes:UP000051427};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN89831.1, ECO:0000313|Proteomes:UP000051427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf231 {ECO:0000313|EMBL:KQN89831.1,
RC ECO:0000313|Proteomes:UP000051427};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQN89831.1}.
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DR EMBL; LMLS01000006; KQN89831.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S9C870; -.
DR STRING; 1736301.ASE95_16815; -.
DR Proteomes; UP000051427; 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; 4.
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 Reference proteome {ECO:0000313|Proteomes:UP000051427};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..761
FT /note="Cytochrome c domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006650851"
FT DOMAIN 38..117
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT REGION 144..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 761 AA; 81054 MW; D3D62719C8745ACF CRC64;
MRRLSFRVRA ACLATAGGAA LVGTIAIGQQ PDGLFTRAQV AAGRDAYGEQ CAACHQPDLA
GATDAPALTG ASFNGVWGKR AIAALYSKIH ASMPYGRGAS LDDATYDAIV AYILYANGAR
AGGTPLDRRS PTLLGAVASG TPPADAFTAP TQDATAATGA PAGSVASQEA QIGGAKEAAP
ANGPGGAAAP ATSAGFAAPG QTVKYADPGR FVLPSKPGLT LKGAIADYRP VTDAMLRDPP
PGDWLMFRRN YQGWSYSPLA QITTGNVAQL QLKWMWSMPE NGTMEDTPIV HDGIMYMWGV
GNVIQALDAR DGELLWENRL GPFPTSAGPG PSSVETRAMG LYGTNLYVNT PEGWVYALDA
RSGAEMWKTH ITDEKPGVGR STGGLIIIKG KVIVGMTNCG RKGTPDHCYI SAYDAATGKR
DWTFTTVALT GQPGGESWGG MPDNDRKGSE TWIAGTYDPE LDTTYWGTAQ GKPWRRDERG
SATGATDYAN STLALDPATG KLKWWFNHAP GETFDLDEVF ERVLVDHGER KSLYTIGKAG
ILWQLDRATG KFVGATETVF QNVFTRIDPV TGRPSYREDV VKQQSDQWLS SCPGPQGGHN
WQAMSYHQPS DALVIPLSQS CVLMLGNGSQ VYYEMPATGG NLGRLSAYRA RDRTPLWSVQ
QRAPFLTSVV STAGNLAFVG DFDRVFRAVD VRTGETLWKT RLGTTVQGFP VSFAVDGHQY
VAVTTALGGG SPQLKPGTML TEVHRPITGY AVYVFGLPER P
//
