ID A0A164CEQ3_9SYNE Unreviewed; 383 AA.
AC A0A164CEQ3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Soluble hydrogenase 42 kDa subunit {ECO:0000313|EMBL:KZR90208.1};
DE EC=1.12.-.- {ECO:0000313|EMBL:KZR90208.1};
GN ORFNames=MITS9508_00756 {ECO:0000313|EMBL:KZR90208.1};
OS Synechococcus sp. MIT S9508.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1801629 {ECO:0000313|EMBL:KZR90208.1, ECO:0000313|Proteomes:UP000076799};
RN [1] {ECO:0000313|EMBL:KZR90208.1, ECO:0000313|Proteomes:UP000076799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT S9508 {ECO:0000313|EMBL:KZR90208.1,
RC ECO:0000313|Proteomes:UP000076799};
RA Cubillos-Ruiz A., Berta-Thompson J.W., Becker J.W., Chisholm S.W.;
RT "Evolutionary Radiation of Lanthipeptides in Marine Picocyanobacteria.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000524-50, ECO:0000256|RuleBase:RU004504};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009236,
CC ECO:0000256|RuleBase:RU004075}.
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:KZR90208.1}.
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; LVHU01000003; KZR90208.1; -; Genomic_DNA.
DR RefSeq; WP_067093761.1; NZ_LVHU01000003.1.
DR AlphaFoldDB; A0A164CEQ3; -.
DR STRING; 1801629.MITS9508_00756; -.
DR PATRIC; fig|1801629.3.peg.818; -.
DR Proteomes; UP000076799; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000313|EMBL:KZR90208.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50}.
FT DOMAIN 19..328
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 337
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 194
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 383 AA; 40947 MW; 356DD547E388DCD0 CRC64;
MQDKLTLMIP GPTPVPETVL KAMGRHPIGH RSGEFQAVVE RTNTQLRWLH QTNSDVLVIT
GSGTAAMEAG IINTLSRGDK VLCGDNGKFG ERWVKVARAY GLDVEVIKAE WGQPLNPDTF
RSALEADTTK SIKAVILTHS ETSTGVINDL QTISGHVKTH GTALTIADCV TSLGAANVPM
DAWGLDVVAS GSQKGYMMPP GLSFVAMSDR AWKGYERSDL PKFYLDLGPY RKTAAKNSNP
FTPAVNLYFA LEAALEMMQT EGLEAIFARH SRHRAASHAA MKAIGLPLFA AEGYGSPAIT
AVAPDGIDAE QLRKAVKDRY DILLAGGQDH LKGKVFRIGH LGFVCDRDVL TAVAAIESVL
QSLGLHKGSM GAGLSAASEI LSQ
//
