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Database: UniProt
Entry: A0A109BK00_HYPSL
LinkDB: A0A109BK00_HYPSL
Original site: A0A109BK00_HYPSL 
ID   A0A109BK00_HYPSL        Unreviewed;       377 AA.
AC   A0A109BK00;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Ferredoxin reductase {ECO:0000313|EMBL:KWT70236.1};
GN   ORFNames=APY04_1061 {ECO:0000313|EMBL:KWT70236.1};
OS   Hyphomicrobium sulfonivorans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Hyphomicrobiaceae; Hyphomicrobium.
OX   NCBI_TaxID=121290 {ECO:0000313|EMBL:KWT70236.1, ECO:0000313|Proteomes:UP000059074};
RN   [1] {ECO:0000313|EMBL:KWT70236.1, ECO:0000313|Proteomes:UP000059074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WDL6 {ECO:0000313|EMBL:KWT70236.1,
RC   ECO:0000313|Proteomes:UP000059074};
RA   Albers P.;
RT   "Transcriptomic analysis of a linuron degrading triple-species bacterial
RT   consortium.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01161}.
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:KWT70236.1}.
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DR   EMBL; LMTR01000033; KWT70236.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A109BK00; -.
DR   STRING; 121290.APY04_1061; -.
DR   PATRIC; fig|121290.4.peg.2261; -.
DR   OMA; KLNICAT; -.
DR   Proteomes; UP000059074; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002641; PNPLA_dom.
DR   PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR   PANTHER; PTHR14226:SF78; SLR0060 PROTEIN; 1.
DR   Pfam; PF01734; Patatin; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS51635; PNPLA; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01161};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|PROSITE-
KW   ProRule:PRU01161};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|PROSITE-
KW   ProRule:PRU01161}; Reference proteome {ECO:0000313|Proteomes:UP000059074}.
FT   DOMAIN          16..208
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
FT   REGION          340..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           20..25
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT   MOTIF           194..196
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        50
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        194
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
SQ   SEQUENCE   377 AA;  41595 MW;  98CDB636C99357D5 CRC64;
     MTEVRRLFRR NVRLNLALQG GGAHGAFTWG VLDRLLEDDE LEISWVSATS AGAVNAVATA
     AGLADGGKAA ARAKLREIWE AVQQAGVPDL MRLNPFLYGL TRTPQLAQMA SMWSPYEFNP
     LGFDPLRRLL SERIDFELLR KQSPIELLIA ATEVSSGRAR LFRRHEMSVD VVLASACLPM
     VHHAVEIDGV AYWDGGFSAN PDLKTLAIDS PVEDTLIVQL NATDRLDLPT GMRDISLHAY
     RLAFDAPLIR EVELIEAVRE CWQGRLGGPR GRLSKLATHR FHLIDAGRYT SALSPESTMK
     PDREMLAHLF EAGKTEADRW LQANRNSIGR RSSVDLKEHF LNPNGRSDNG VFSEGGVSER
     PSVNANGKAA RDIPEGI
//
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