ID A0A1V3RMH0_9BACT Unreviewed; 847 AA.
AC A0A1V3RMH0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Dehydrogenase {ECO:0000313|EMBL:OOG78054.1};
GN ORFNames=B0E43_02790 {ECO:0000313|EMBL:OOG78054.1};
OS Algoriphagus sp. A40.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=1945863 {ECO:0000313|EMBL:OOG78054.1, ECO:0000313|Proteomes:UP000188460};
RN [1] {ECO:0000313|EMBL:OOG78054.1, ECO:0000313|Proteomes:UP000188460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A40 {ECO:0000313|EMBL:OOG78054.1,
RC ECO:0000313|Proteomes:UP000188460};
RA Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA Frostegard A.;
RT "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT isolation strategy.";
RL Submitted (FEB-2017) 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:OOG78054.1}.
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DR EMBL; MUNY01000035; OOG78054.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3RMH0; -.
DR STRING; 1945863.B0E43_02790; -.
DR OrthoDB; 9808161at2; -.
DR Proteomes; UP000188460; 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; 1.25.10.10; Leucine-rich Repeat Variant; 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; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
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 SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR PROSITE; PS51007; CYTC; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..847
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012392376"
FT DOMAIN 709..803
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 847 AA; 94226 MW; 2E2FEE52AA0B8C36 CRC64;
MLRSSFFCCA VVLMFFFACK EPGPLPETPD SPTRTAEEEA GTFQIEPGFE IQLVASEPLV
ESPVIIQFDE DGRLWVVEMR GYMNDMEGSE EKQPVGSVAI LEDTDGDGEM DKRTVYLDSL
IMPRALGLFK TGALIAENNA LWITQDLDGD WKADSKILLD STYAANGIPE HSDNGFVRNV
DNWYYSAKSS LRYRFQEGTW IRDSTEFRGQ WGISQDDQGR LIYNYNWSQL HGDLVPANYL
SRNKNHKPST GIDHGFTIDR KVFPIRTNPA VNRGYIPGTL DSAGRLLEFT SASAPTVYRS
HLFPKEYLGN VFVMENAGNL VKRNVVTEKG ILLEAQDPNP GREFLASTDE RFRPVHATVG
PDGGLYLVDM YQGIVQHGSY MTPYLKEQTK KRGLDSPGHM GRIWRVVPKG FDPKPFPKLS
HASYLELVKY LSHQDGWFRD MAQQILVERK DPASVAQLIE LIKNGESELG KFHAMWSLEG
MGKVNPDLLL EVLKSGSNLL QTTALRQLEK PALSDSVLLF RLEKVISELS ENFSEHLALQ
LALSAEVLGK ETKVDLLSQI IEKYGNLALI RDAVLSSLEG QEYDFLQKLA AEKSWKEASS
DKEIFLEMLT TAVVNNGNSE EISGLLTLAD EPEMGWKETV ILTGMAIKAA DAETPGLVSL
KSSPKIFSRS DLPLEQNRVE MLKRLFSWPG HQPSSTIALA GNLDEKAMKQ FANGRQKYMV
SCAGCHGSNG KGIARMGPPL VGSEWVLGNE IRLALILLHG IEGPIEVSGK KYDAPEILPV
MPSHSTMDDG DIAAILTYIR NEWGNQAPPV TGRTVSSTRH LNQGRVYPWS AVELKKHMEN
LASAPKP
//
