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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//