ID G1C7G7_9GAMM Unreviewed; 472 AA.
AC G1C7G7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Rubredoxin-like domain-containing protein {ECO:0000259|PROSITE:PS50903};
OS Alcanivorax hongdengensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alcanivorax.
OX NCBI_TaxID=519051 {ECO:0000313|EMBL:AEK10593.1};
RN [1] {ECO:0000313|EMBL:AEK10593.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A-11-3 {ECO:0000313|EMBL:AEK10593.1};
RA Wang W.;
RT "Genes Involved in Alkane Degradation in Alcanivorax hongdengensis Strain
RT A-11-3.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family. AlkB
CC subfamily. {ECO:0000256|ARBA:ARBA00010823}.
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DR EMBL; JF747236; AEK10593.1; -; Genomic_DNA.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd03512; Alkane-hydroxylase; 1.
DR CDD; cd00730; rubredoxin; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR InterPro; IPR033885; AlkB/XylM.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR024934; Rubredoxin-like_dom.
DR InterPro; IPR024935; Rubredoxin_dom.
DR InterPro; IPR018527; Rubredoxin_Fe_BS.
DR PANTHER; PTHR38674; ALKANE 1-MONOOXYGENASE 1; 1.
DR PANTHER; PTHR38674:SF1; ALKANE 1-MONOOXYGENASE 1; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR Pfam; PF00301; Rubredoxin; 1.
DR PRINTS; PR00163; RUBREDOXIN.
DR SUPFAM; SSF57802; Rubredoxin-like; 1.
DR PROSITE; PS00202; RUBREDOXIN; 1.
DR PROSITE; PS50903; RUBREDOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Iron {ECO:0000256|ARBA:ARBA00023004}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023033};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 18..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 85..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 418..470
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50903"
SQ SEQUENCE 472 AA; 53895 MW; 6593C03656F51967 CRC64;
MATLEQGNAT PWHDGKRYLW LLSPAIPVLA VLFLALYMFA WSWPGLLWGG PFLVYALIPF
ADWVVGTDTN NPPESAVQQL EDDKYYRLIV YAYIPTQYLA TFMGAWLVAQ GDTPLWGLVG
LVFSVGAVNG IAINTAHELG HKKGKSERXL AKITLAPVAY GHFFVEHNKG HHKNVATPED
PASSRMGESF WAFLPRTMIG SVKSAWGIEK QRLERCQQPL WSLKNENLQS WLMTVVLFGA
LTVWFGWVVL PFLLLQAFYG ASLLEVINYM EHYGLLRQQK ADGRYERCEP RHSWNSNHIV
TNLFLYQLQR HSDHHANPTR RFQALRHFDD SPQLPSGYAS MLIPAYIPFV WFQKMNPPVY
QHYQGDLSRA NLQPGKRDKL LAKWQQAPVQ YKSADSEPDY SREALLAARE AEKETDITHR
FECPNCGYIY DEAQGNDSEG FPAGTRWAQI PDNWPCPDCG IPEKIDFVLK QH
//
