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Database: UniProt
Entry: A4CWP6_SYNPV
LinkDB: A4CWP6_SYNPV
Original site: A4CWP6_SYNPV 
ID   A4CWP6_SYNPV            Unreviewed;       383 AA.
AC   A4CWP6;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Soluble hydrogenase small subunit {ECO:0000313|EMBL:EAR17696.1};
GN   ORFNames=WH7805_09209 {ECO:0000313|EMBL:EAR17696.1};
OS   Synechococcus sp. (strain WH7805).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=59931 {ECO:0000313|EMBL:EAR17696.1, ECO:0000313|Proteomes:UP000001224};
RN   [1] {ECO:0000313|EMBL:EAR17696.1, ECO:0000313|Proteomes:UP000001224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH7805 {ECO:0000313|Proteomes:UP000001224};
RA   Scanlan D., Ostrowski M., Mazard S., Wilkinson N., Partensky F.,
RA   Dufresne A., Garczarek L., Hess W., Gierga G., Voss B., Axmann I., Post A.,
RA   Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K., Beeson K.,
RA   Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (FEB-2006) 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:EAR17696.1}.
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DR   EMBL; AAOK01000005; EAR17696.1; -; Genomic_DNA.
DR   RefSeq; WP_006042642.1; NZ_CH724168.1.
DR   AlphaFoldDB; A4CWP6; -.
DR   STRING; 59931.WH7805_09209; -.
DR   eggNOG; COG0075; Bacteria.
DR   HOGENOM; CLU_027686_1_1_3; -.
DR   OrthoDB; 389074at2; -.
DR   PhylomeDB; A4CWP6; -.
DR   Proteomes; UP000001224; Unassembled WGS sequence.
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   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;  40823 MW;  2042B8E94486CED7 CRC64;
     MQDKLTLMIP GPTPVPETVL KAMGRHPIGH RSGEFQAVVE RTNAQLRWLH QTSSDVLVIT
     GSGTAAMEAG IINTLSRGDR VLCGDNGKFG ERWVKVARAY GLDVDVIKAE WGQPLDPEAF
     RTALEADTDK TIKAVILTHS ETSTGVINDL QTISSYVKAH GVALTIADCV TSLGATNVPM
     DAWGLDVVAS GSQKGYMMPP GLSFVAMSDR AWTAYERSDL PKFYLDLGPY RKTAAKNSNP
     FTPAVNLYFA LDAALEMMQS EGLEAIFARH ARHRAAATAA MKAIGLPLFA AEGYGSPAIT
     AVAPDGIDAE QLRKAVKERF DILLAGGQDH LKGHVFRIGH LGFVCDRDVL TAVAAIESVL
     QSLGLHKGEM GAGLSAASLA LGN
//
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