ID A0A0A7PKB7_9SPHN Unreviewed; 728 AA.
AC A0A0A7PKB7;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Alcohol dehydrogenase [cytochrome c] {ECO:0000313|EMBL:AJA10450.1};
DE EC=1.1.2.8 {ECO:0000313|EMBL:AJA10450.1};
GN Name=adh {ECO:0000313|EMBL:AJA10450.1};
GN ORFNames=SKP52_17900 {ECO:0000313|EMBL:AJA10450.1};
OS Sphingopyxis fribergensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1515612 {ECO:0000313|EMBL:AJA10450.1, ECO:0000313|Proteomes:UP000030907};
RN [1] {ECO:0000313|EMBL:AJA10450.1, ECO:0000313|Proteomes:UP000030907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kp5.2 {ECO:0000313|EMBL:AJA10450.1,
RC ECO:0000313|Proteomes:UP000030907};
RX PubMed=26040579; DOI=10.1099/ijs.0.000371;
RA Oelschlagel M., Ruckert C., Kalinowski J., Schmidt G., Schlomann M.,
RA Tischler D.;
RT "Description of Sphingopyxis fribergensis sp. nov. - a soil bacterium with
RT the ability to degrade styrene and phenylacetic acid.";
RL Int. J. Syst. Evol. Microbiol. 65:3008-3015(2015).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR617512-3};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR617512-3};
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000256|PIRSR:PIRSR617512-2};
CC Note=Binds 1 heme c group per subunit. {ECO:0000256|PIRSR:PIRSR617512-
CC 2};
CC -!- COFACTOR:
CC Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC Evidence={ECO:0000256|PIRSR:PIRSR617512-2};
CC Note=Binds 1 PQQ group per subunit. {ECO:0000256|PIRSR:PIRSR617512-2};
CC -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008156}.
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; CP009122; AJA10450.1; -; Genomic_DNA.
DR RefSeq; WP_039576934.1; NZ_CP009122.1.
DR AlphaFoldDB; A0A0A7PKB7; -.
DR STRING; 1515612.SKP52_17900; -.
DR KEGG; sphk:SKP52_17900; -.
DR HOGENOM; CLU_018478_0_1_5; -.
DR OrthoDB; 9794322at2; -.
DR Proteomes; UP000030907; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0052934; F:alcohol dehydrogenase (cytochrome c) activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR CDD; cd10279; PQQ_ADH_II; 1.
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; IPR017512; PQQ_MeOH/EtOH_DH.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR NCBIfam; TIGR03075; PQQ_enz_alc_DH; 1.
DR PANTHER; PTHR32303; QUINOPROTEIN ALCOHOL DEHYDROGENASE (CYTOCHROME C); 1.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR Pfam; PF13360; PQQ_2; 2.
DR SMART; SM00564; PQQ; 6.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS51007; CYTC; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR617512-3};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR617512-4};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR617512-2};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR617512-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR617512-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AJA10450.1}; PQQ {ECO:0000256|PIRSR:PIRSR617512-2};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..728
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002031860"
FT DOMAIN 633..712
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT ACT_SITE 337
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-1"
FT BINDING 96
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 148
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 192
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 208..209
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 272
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 292
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 337
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 364
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 427..428
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 646
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 649
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 650
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 689
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT DISULFID 142..143
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-4"
SQ SEQUENCE 728 AA; 77329 MW; AC251200F560D053 CRC64;
MAKRVWTAAL LGGAALALAS CNASKNDSIS GGASLDAAEK ASETLLKTGG NGDDWAGIGY
SYDEQRFSPL TDINDQNVGQ LGIAWTADLD DARGQEATPV VVDGVMYVTH AWSKVSAWDA
ATGKSLWKFD PKVPGERAVS ACCDVVNRGV AVWGDKVFVG ALDGRLIALD KRTGQEIWAT
QTFDTSKPYT ITGAPRVVKD MVLIGNGGAE FGVRGYVTAY DADTGKKRWR FYTAPNPTKA
KDGAASDDIF ASKANATWSD QGEWQTSGGG GTVWDAIVYD KDLDQIYLGV GNGNPWNHGT
RSNGEGDNWF LSSVVALDAM TGKYKWHYQE TPGETWDYTA TQPIILAEQA VNGTPTKVLY
HAPKNGFFFT IDRNNGKLID AKPFVDGINW ATGYDMATGR PIETPESRFY KTGKPFIAIP
GALGAHNWHP MSYNPATGLV YIPAQQIPQG YLADMTELDK RKVVGFNIGA SLTATMLPDD
KAAYRAAVAA TTGRLVAFDP RTGKVAWAVD HPAAWNGGTM TTAGNLVFQG TSLGRFRAYA
ADTGKQLLDL DMQSGIVSAP STFRVGGVQY IAFQTSKGGA FPLVAGVAGG ATRKIPNIPR
LIVLKIGGTM KLPAPPPTTT LAWNPPPMTA SPAQVAAGKA HFGRYCIVCH GDSAIGNGFT
PDLRVSGTLA NADAWKGVVI GGALKDRGMV SFANVLTPAD AEAIRAYVIE RSNWTKANLA
DSAAPMGR
//
