ID A0A1H8MGW1_9RHOB Unreviewed; 562 AA.
AC A0A1H8MGW1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Dehydrogenase, PQQ-dependent, s-GDH family {ECO:0000313|EMBL:SEO16396.1};
GN ORFNames=SAMN04489859_10405 {ECO:0000313|EMBL:SEO16396.1};
OS Paracoccus alcaliphilus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=34002 {ECO:0000313|EMBL:SEO16396.1, ECO:0000313|Proteomes:UP000199054};
RN [1] {ECO:0000313|EMBL:SEO16396.1, ECO:0000313|Proteomes:UP000199054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8512 {ECO:0000313|EMBL:SEO16396.1,
RC ECO:0000313|Proteomes:UP000199054};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000256|ARBA:ARBA00001926};
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DR EMBL; FODE01000040; SEO16396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8MGW1; -.
DR STRING; 34002.SAMN04489859_10405; -.
DR Proteomes; UP000199054; Unassembled WGS sequence.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR008168; Cyt_C_IC.
DR InterPro; IPR012938; Glc/Sorbosone_DH.
DR InterPro; IPR019893; PQQ-dependent_DH_s-GDH.
DR InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
DR NCBIfam; TIGR03606; non_repeat_PQQ; 1.
DR PANTHER; PTHR19328; HEDGEHOG-INTERACTING PROTEIN; 1.
DR PANTHER; PTHR19328:SF13; HIPL1 PROTEIN; 1.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR Pfam; PF07995; GSDH; 2.
DR PRINTS; PR00605; CYTCHROMECIC.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 4: Predicted;
KW Electron transport {ECO:0000256|ARBA:ARBA00022660};
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}; Reference proteome {ECO:0000313|Proteomes:UP000199054};
KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660};
KW Transport {ECO:0000256|ARBA:ARBA00022660}.
FT DOMAIN 471..546
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT REGION 424..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 562 AA; 60869 MW; 4767BE6591B54C31 CRC64;
MIWVTERTSG EVTRVDPTTG AQQVLLAIDG VYIGPQHEGL LGMALHPELM QGQDNDHVYL
SYTINNGSAD DPDPTAQIVR YSYDEQLQQL VDPVILIEGL PAWNDHNAGR VVFGPDNMLY
YSIGDQGANF GRNQRRENLA STLPTQEEVD DSNWRTYSGK ILRLNLDGTI PDDNPELVGV
RSHVYSYGHR NPQGLAFGSN GKLYETEHGP ATDDELNIIE AGGNYGWPWV AGKMDDSAYL
YVNWSEAPDD VNVNAIPVPD TVPQFPESDF DGEIIEPVAT YWTVEDGYPI GEICGYICDP
TIAPSSVYYY EASEDGIAEW DNSVLIPTLK HGALYVQPLS EDGTEAASAP IAWLSTQNRY
RDVIVGPDNR TVFIATDAFG SASQKYGQGL NTSVLHNPGA ILTFTYGDDG NVTRFAEAPI
TVDEAQLASS STDAPQEWED PATRSDERPE SAAVTTGEAD VSVTEDSNIA EVAALGAPKY
ADSCAMCHGP AGGGGAGAVL AGNKQLDDIQ FVANSIVHGF GYMPSFGSQL NDNDIAEIST
FIRNSWGNEF GVLTTEQVQT VR
//
