ID A0A0R2TMM4_9RHOB Unreviewed; 510 AA.
AC A0A0R2TMM4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Phytoene dehydrogenase {ECO:0000313|EMBL:KRO88524.1};
GN ORFNames=ABR89_09025 {ECO:0000313|EMBL:KRO88524.1};
OS Rhodobacter sp. BACL10 MAG-120910-bin24.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=1655597 {ECO:0000313|EMBL:KRO88524.1, ECO:0000313|Proteomes:UP000051243};
RN [1] {ECO:0000313|EMBL:KRO88524.1, ECO:0000313|Proteomes:UP000051243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL7 MAG-120910-bin24 {ECO:0000313|EMBL:KRO88524.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Carotenoid biosynthesis. {ECO:0000256|ARBA:ARBA00004829,
CC ECO:0000256|RuleBase:RU362075}.
CC -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00006046, ECO:0000256|RuleBase:RU362075}.
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:KRO88524.1}.
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DR EMBL; LICH01000074; KRO88524.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2TMM4; -.
DR Proteomes; UP000051243; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR014105; Carotenoid/retinoid_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR NCBIfam; TIGR02734; crtI_fam; 1.
DR PANTHER; PTHR43734:SF3; B-CAROTENE KETOLASE; 1.
DR PANTHER; PTHR43734; PHYTOENE DESATURASE; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Carotenoid biosynthesis {ECO:0000256|ARBA:ARBA00022746,
KW ECO:0000256|RuleBase:RU362075}; Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362075};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..496
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 510 AA; 57476 MW; 9213AC31778D9108 CRC64;
MKKQNYTNLC NVNSPPSGSV LVIGAGFGGI AVALRMRAKG FNVTLVDRLQ SIGGRAQVFE
RGGFRHDAGP TVITAPFLFD ELFNLFGEKR SDHVEFRSLD PWYRFYFHGG RQFDYRRSIE
DTNAEILKFE KSDVEGYAQL LKTSKEIFEV GFNKLADRPF HKISTMLAQI PKLLHLKSYY
SVVGIVNKHI KHPMLRQAFS IHPLLVGGNP FTTTSIYALI HYLERRWGVF FCMGGTGRLV
SALHALLIRV GVKVELGIDI TEITLKNGRA TGAVSKEGKE FFADRVICNG DPPTVYAQML
PADGNRRKRL ASDRITQYSM GLYVLFFGTT RKYPDIAHHT IWMGPRYKEL LEDIFDKKIL
SEDFSLYVHR PTATDDSFAP VGCDSFYVLC PVPNLRGNID WADKAPKLRD RIVSALSDTI
MPDLAAVITD DFWMTPEDFK KNYRSMYGAG FSIAPIFTQS AWFRYHNRDP HIPNLYFAAA
GAHPGAGMPG VLCSAKVVEK LIDQELQGHH
//
