ID B1XMM6_PICP2 Unreviewed; 454 AA. AC B1XMM6; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAR-2024, entry version 98. DE SubName: Full=Succinate-semialdehyde dehydrogenase {ECO:0000313|EMBL:ACB00745.1}; GN OrderedLocusNames=SYNPCC7002_A2771 {ECO:0000313|EMBL:ACB00745.1}; OS Picosynechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum OS quadruplicatum). OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae; OC Chroococcales; Geminocystaceae; Picosynechococcus. OX NCBI_TaxID=32049 {ECO:0000313|EMBL:ACB00745.1, ECO:0000313|Proteomes:UP000001688}; RN [1] {ECO:0000313|Proteomes:UP000001688} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27264 / PCC 7002 / PR-6 RC {ECO:0000313|Proteomes:UP000001688}; RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T., RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J., RA Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.; RT "Complete sequence of Synechococcus sp. PCC 7002."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0007829|PDB:4IT9, ECO:0007829|PDB:4ITA} RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH NADPH. RX PubMed=23589281; DOI=10.1074/jbc.M113.460428; RA Park J., Rhee S.; RT "Structural basis for a cofactor-dependent oxidation protection and RT catalysis of cyanobacterial succinic semialdehyde dehydrogenase."; RL J. Biol. Chem. 288:15760-15770(2013). RN [3] {ECO:0007829|PDB:3VZ1, ECO:0007829|PDB:3VZ2} RP X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) IN COMPLEX WITH NADP(+). RX PubMed=23500184; DOI=10.1016/j.jsb.2013.03.001; RA Yuan Z., Yin B., Wei D., Yuan Y.R.; RT "Structural basis for cofactor and substrate selection by cyanobacterium RT succinic semialdehyde dehydrogenase."; RL J. Struct. Biol. 182:125-135(2013). CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00009986}. 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; CP000951; ACB00745.1; -; Genomic_DNA. DR RefSeq; WP_012308363.1; NZ_JAHHPU010000003.1. DR PDB; 3VZ1; X-ray; 2.10 A; A/B=1-454. DR PDB; 3VZ2; X-ray; 2.50 A; A/B=1-454. DR PDB; 3VZ3; X-ray; 1.69 A; A/B=1-454. DR PDB; 4IT9; X-ray; 1.70 A; A/B=1-454. DR PDB; 4ITA; X-ray; 1.40 A; A/B=1-454. DR PDB; 4ITB; X-ray; 1.40 A; A/B=1-454. DR PDBsum; 3VZ1; -. DR PDBsum; 3VZ2; -. DR PDBsum; 3VZ3; -. DR PDBsum; 4IT9; -. DR PDBsum; 4ITA; -. DR PDBsum; 4ITB; -. DR AlphaFoldDB; B1XMM6; -. DR SMR; B1XMM6; -. DR STRING; 32049.SYNPCC7002_A2771; -. DR KEGG; syp:SYNPCC7002_A2771; -. DR eggNOG; COG1012; Bacteria. DR HOGENOM; CLU_005391_1_0_3; -. DR BioCyc; MetaCyc:MONOMER-17041; -. DR BRENDA; 1.2.1.79; 6187. DR Proteomes; UP000001688; Chromosome. DR GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IEA:InterPro. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR CDD; cd07100; ALDH_SSADH1_GabD1; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR InterPro; IPR044148; ALDH_GabD1-like. DR InterPro; IPR047110; GABD/Sad-like. DR PANTHER; PTHR43217; SUCCINATE SEMIALDEHYDE DEHYDROGENASE [NAD(P)+] SAD; 1. DR PANTHER; PTHR43217:SF1; SUCCINATE SEMIALDEHYDE DEHYDROGENASE [NAD(P)+] SAD; 1. DR Pfam; PF00171; Aldedh; 1. DR SUPFAM; SSF53720; ALDH-like; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:3VZ1, ECO:0007829|PDB:3VZ2}; KW Nucleotide-binding {ECO:0007829|PDB:3VZ3, ECO:0007829|PDB:4ITA}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Reference proteome {ECO:0000313|Proteomes:UP000001688}. FT DOMAIN 3..451 FT /note="Aldehyde dehydrogenase" FT /evidence="ECO:0000259|Pfam:PF00171" FT BINDING 128 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007829|PDB:3VZ3" FT BINDING 128 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4ITA" FT BINDING 128 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4ITB" FT BINDING 130 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007829|PDB:3VZ3" FT BINDING 130 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4ITB" FT BINDING 131 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4ITB" FT BINDING 139 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007829|PDB:3VZ3" FT BINDING 139 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4ITA" FT BINDING 154 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007829|PDB:3VZ3" FT BINDING 154 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4ITB" FT BINDING 154 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4ITA" FT BINDING 157 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007829|PDB:3VZ3" FT BINDING 157 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4ITB" FT BINDING 157 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4ITA" FT BINDING 206 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007829|PDB:3VZ3" FT BINDING 206 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4ITB" FT BINDING 207 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007829|PDB:3VZ3" FT BINDING 207 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4ITA" FT BINDING 207 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4ITB" FT BINDING 213 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4ITB" FT BINDING 228 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007829|PDB:3VZ3" FT BINDING 228 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4ITA" FT BINDING 228 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4ITB" FT BINDING 229 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007829|PDB:3VZ3" FT BINDING 229 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4ITB" FT BINDING 229 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4ITA" FT BINDING 262 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="2" FT /ligand_note="covalent" FT /evidence="ECO:0007829|PDB:4ITA" FT BINDING 359 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0007829|PDB:3VZ3" FT BINDING 359 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4ITB" FT BINDING 359 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4ITA" SQ SEQUENCE 454 AA; 49019 MW; 775446BD8C9D6CB6 CRC64; MAIATINPTT GEICQRFKAL TPAEIDAKLA KAQEAFQAYR RTSFSQRRQW LENAAAILER DTSKFAEIMT TEMGKTHQSA IAEAEKSALV CRYYAEHGEQ FLANEYTETQ ATESYVCYQP LGILLAVMPW NFPFWQVFRF AAPALMAGNV AVLKHASNVP QCALAVEAIL EAAGFPEGVF QTLLIGASQV EQVIKDPRVK AATLTGSEPA GASLASLAGQ EIKPTLLELG GSDPFVVFPS ADLDEAVEVG TVARTMNNGQ SCIAAKRFIL HEAIAAEFLE KLHLKFASLK IGDPMAPETD IGPLATEGIL QDISRQVDQA VAAGAKILLG GRPLDRAGYF YPPTILTEIP PGAKILQEEL FAPVAMVFTV KDLDQAIALA NDIPFGLGAS AWTNDPAEQQ RFIQELDAGA VFINGMVKSD PRLPFGGTKR SGYGRELGLA GIRTFVNAKT VWLK //