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Database: UniProt
Entry: H1G632_9GAMM
LinkDB: H1G632_9GAMM
Original site: H1G632_9GAMM 
ID   H1G632_9GAMM            Unreviewed;       512 AA.
AC   H1G632;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Amine oxidase {ECO:0000313|EMBL:EHQ53269.1};
GN   ORFNames=ECTPHS_11315 {ECO:0000313|EMBL:EHQ53269.1};
OS   Ectothiorhodospira sp. PHS-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Ectothiorhodospira.
OX   NCBI_TaxID=519989 {ECO:0000313|EMBL:EHQ53269.1, ECO:0000313|Proteomes:UP000005314};
RN   [1] {ECO:0000313|EMBL:EHQ53269.1, ECO:0000313|Proteomes:UP000005314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHS-1 {ECO:0000313|EMBL:EHQ53269.1,
RC   ECO:0000313|Proteomes:UP000005314};
RA   Saltikov C.W., Zargar K., Conrad A., Bernick D., Lowe T.M., Stolc V.,
RA   Hoeft S., Oremland R.S., Stolz J.;
RT   "ArxA, a new clade of arsenite oxidase within the DMSO family of molybdenum
RT   oxidoreductases.";
RL   Submitted (JAN-2012) 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:EHQ53269.1}.
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DR   EMBL; AGBG01000027; EHQ53269.1; -; Genomic_DNA.
DR   RefSeq; WP_008932836.1; NZ_AGBG01000027.1.
DR   AlphaFoldDB; H1G632; -.
DR   STRING; 519989.ECTPHS_11315; -.
DR   PATRIC; fig|519989.5.peg.2220; -.
DR   eggNOG; COG1233; Bacteria.
DR   OrthoDB; 9774675at2; -.
DR   Proteomes; UP000005314; Unassembled WGS sequence.
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};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362075}.
FT   DOMAIN          28..496
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   512 AA;  57119 MW;  F3271F0FF10F8265 CRC64;
     MVEPHSATAS SHANPDAPHA VVIGSGFGGL AAAIRLGARG YRVTVLEKLD APGGRAYVFR
     KDGFTFDAGP TIVTAPFVLE ELWQLCGRRM EDDVDLRPMD PFYQIRFHDG EVFNYWADVE
     AVRAEVARFS PDDLNGYDAY MRDSEANYRV GFEKLAHVPF NSWTDMAKVV PELLRLRADR
     SVCGLVAKHI KNPRLQQVLS FHPLLVGGNP FRTTSAYTLI SYLERRFGVH SAMGGTGHIV
     KGLVGLIEGQ GNVVRCNQEV RQILVENGRA TGVRLASGET IAADVVVSNA DSAATYRYLV
     PESARRKWTN RRIERSRYSM SLMVWYFGTK KRYEDVPHHS IILGPRYREL LDDIFDRKVL
     AEDFSLYLHR PTKTDPSLAP EGCDTFYVLS PVPHMESGVD WQQQAEPYRR KIEQYLSEHV
     LPDLENQVVA SHMITPPYFQ NTLSSFRGAA FGLEPILTQS AWFRPHNQSE DVDRLYLVGA
     GTHPGAGLPG VISSAKVLDR VVPDAATIKG AS
//
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