ID A0A1R4HAL9_9GAMM Unreviewed; 604 AA.
AC A0A1R4HAL9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Methylamine utilization protein MauG {ECO:0000313|EMBL:SJM93071.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:SJM93071.1};
GN Name=mauG {ECO:0000313|EMBL:SJM93071.1};
GN ORFNames=CRENPOLYSF1_380016 {ECO:0000313|EMBL:SJM93071.1};
OS Crenothrix polyspora.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Crenotrichaceae; Crenothrix.
OX NCBI_TaxID=360316 {ECO:0000313|EMBL:SJM93071.1, ECO:0000313|Proteomes:UP000195667};
RN [1] {ECO:0000313|EMBL:SJM93071.1, ECO:0000313|Proteomes:UP000195667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSM_CP1 {ECO:0000313|EMBL:SJM93071.1};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SCO1/2 family.
CC {ECO:0000256|ARBA:ARBA00010996}.
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DR EMBL; FUKI01000113; SJM93071.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4HAL9; -.
DR OrthoDB; 9805202at2; -.
DR Proteomes; UP000195667; 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 CDD; cd02968; SCO; 1.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR004852; Di-haem_cyt_c_peroxidsae.
DR InterPro; IPR003782; SCO1/SenC.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR30600; CYTOCHROME C PEROXIDASE-RELATED; 1.
DR Pfam; PF03150; CCP_MauG; 1.
DR Pfam; PF02630; SCO1-SenC; 1.
DR SUPFAM; SSF46626; Cytochrome c; 2.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51007; CYTC; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|PIRSR:PIRSR603782-1};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
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,
KW ECO:0000256|PIRSR:PIRSR603782-1};
KW Oxidoreductase {ECO:0000313|EMBL:SJM93071.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000195667}.
FT DOMAIN 38..230
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 271..381
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 425..584
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 95
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 101
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 194
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 95..101
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 604 AA; 67066 MW; 407E483D3BA2212B CRC64;
MIAQQLLRKI GWLIIILVNA RSYADTSPPT LAPGYGNLQF TAPEPDSYTL PPLGQAADGK
VLDIEGHDTS LHALIGDKAK ATDKIVLLSF IYATCSDVNG CPLATTVLHK INSRLQKEPE
LAKKLRLLTL SFNPAHDTPA QMKHYGASLQ DGTLEWHFLT TRSEQELNPI LNAYQQNIQK
IYDDKGQDTG TFSHVLRVYL IDQQRQIRSI YSLSFLHPDT VINDIKSLLQ KPTAKTPPSP
LKTIDALKTI KHPPLGLPPV PIPDNNPISL QKVSLGKKLF FDRRLSLNNT MSCAMCHIAD
QGFTNNQMAT AVGAEGRTVR RNSPSLYNTG YFSLLFHDGR ETSLEQQVWL PLLTHNEMAN
PSIGYVIDKI NTSADYTGLF QKAFKKPASM ETVGMALASY ERTLNSANSP FDRWQYGHDQ
QALDAKAQRG YQLFIGKAAC SQCHTVGDKH ALFTDNSLHN TGIGYRDAMV SNDNKQSVQL
APGVFVNVDA QLLASVSETK TNDLGRYEIT QNPAHRWQYK TPSLRNIQLT APYMHNGSLA
SLQEVIAFYN QGGIANENRD PLIKPLHLSD EESKDLAYFL TQLTGDNVQE LIDEARTAPV
GDRQ
//
