ROCA1_ALKHC
ID ROCA1_ALKHC Reviewed; 515 AA.
AC Q9K9B2;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=1-pyrroline-5-carboxylate dehydrogenase 1;
DE Short=P5C dehydrogenase 1;
DE EC=1.2.1.88;
DE AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase;
GN Name=rocA1; OrderedLocusNames=BH2737;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-
CC glutamate + NADH; Xref=Rhea:RHEA:30235, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58066; EC=1.2.1.88;
CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC glutamate; L-glutamate from L-proline: step 2/2.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. RocA
CC subfamily. {ECO:0000305}.
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DR EMBL; BA000004; BAB06456.1; -; Genomic_DNA.
DR PIR; A83992; A83992.
DR RefSeq; WP_010898885.1; NC_002570.2.
DR PDB; 3QAN; X-ray; 1.95 A; A/B/C=1-515.
DR PDBsum; 3QAN; -.
DR AlphaFoldDB; Q9K9B2; -.
DR SMR; Q9K9B2; -.
DR STRING; 272558.10175358; -.
DR EnsemblBacteria; BAB06456; BAB06456; BAB06456.
DR KEGG; bha:BH2737; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_0_9; -.
DR OMA; NWNKQLT; -.
DR OrthoDB; 744602at2; -.
DR BRENDA; 1.2.1.88; 661.
DR UniPathway; UPA00261; UER00374.
DR Proteomes; UP000001258; Chromosome.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniPathway.
DR CDD; cd07124; ALDH_PutA-P5CDH-RocA; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR HAMAP; MF_00733; RocA; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR005932; RocA.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR01237; D1pyr5carbox2; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..515
FT /note="1-pyrroline-5-carboxylate dehydrogenase 1"
FT /id="PRO_0000056507"
FT ACT_SITE 286
FT /evidence="ECO:0000250"
FT ACT_SITE 320
FT /evidence="ECO:0000250"
FT HELIX 16..32
FT /evidence="ECO:0007829|PDB:3QAN"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:3QAN"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:3QAN"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:3QAN"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:3QAN"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:3QAN"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:3QAN"
FT HELIX 72..89
FT /evidence="ECO:0007829|PDB:3QAN"
FT HELIX 94..110
FT /evidence="ECO:0007829|PDB:3QAN"
FT HELIX 112..122
FT /evidence="ECO:0007829|PDB:3QAN"
FT HELIX 127..152
FT /evidence="ECO:0007829|PDB:3QAN"
FT STRAND 163..171
FT /evidence="ECO:0007829|PDB:3QAN"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:3QAN"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:3QAN"
FT HELIX 186..197
FT /evidence="ECO:0007829|PDB:3QAN"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:3QAN"
FT HELIX 211..223
FT /evidence="ECO:0007829|PDB:3QAN"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:3QAN"
FT TURN 238..241
FT /evidence="ECO:0007829|PDB:3QAN"
FT HELIX 242..247
FT /evidence="ECO:0007829|PDB:3QAN"
FT STRAND 251..258
FT /evidence="ECO:0007829|PDB:3QAN"
FT HELIX 260..270
FT /evidence="ECO:0007829|PDB:3QAN"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:3QAN"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:3QAN"
FT HELIX 301..313
FT /evidence="ECO:0007829|PDB:3QAN"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:3QAN"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:3QAN"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:3QAN"
FT HELIX 333..344
FT /evidence="ECO:0007829|PDB:3QAN"
FT HELIX 365..381
FT /evidence="ECO:0007829|PDB:3QAN"
FT STRAND 382..386
FT /evidence="ECO:0007829|PDB:3QAN"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:3QAN"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:3QAN"
FT HELIX 411..414
FT /evidence="ECO:0007829|PDB:3QAN"
FT STRAND 419..429
FT /evidence="ECO:0007829|PDB:3QAN"
FT HELIX 430..438
FT /evidence="ECO:0007829|PDB:3QAN"
FT STRAND 440..449
FT /evidence="ECO:0007829|PDB:3QAN"
FT HELIX 453..462
FT /evidence="ECO:0007829|PDB:3QAN"
FT STRAND 466..472
FT /evidence="ECO:0007829|PDB:3QAN"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:3QAN"
FT TURN 499..501
FT /evidence="ECO:0007829|PDB:3QAN"
FT HELIX 502..505
FT /evidence="ECO:0007829|PDB:3QAN"
FT STRAND 506..514
FT /evidence="ECO:0007829|PDB:3QAN"
SQ SEQUENCE 515 AA; 56642 MW; 1AA5F76CA3093749 CRC64;
MLQPYKHEPF TDFTVEANRK AFEEALGLVE KELGKEYPLI INGERVTTED KIQSWNPARK
DQLVGSVSKA NQDLAEKAIQ SADEAFQTWR NVNPEERANI LVKAAAIIRR RKHEFSAWLV
HEAGKPWKEA DADTAEAIDF LEYYARQMIE LNRGKEILSR PGEQNRYFYT PMGVTVTISP
WNFALAIMVG TAVAPIVTGN TVVLKPASTT PVVAAKFVEV LEDAGLPKGV INYVPGSGAE
VGDYLVDHPK TSLITFTGSK DVGVRLYERA AVVRPGQNHL KRVIVEMGGK DTVVVDRDAD
LDLAAESILV SAFGFSGQKC SAGSRAVIHK DVYDEVLEKT VALAKNLTVG DPTNRDNYMG
PVIDEKAFEK IMSYIEIGKK EGRLMTGGEG DSSTGFFIQP TIIADLDPEA VIMQEEIFGP
VVAFSKANDF DHALEIANNT EYGLTGAVIT RNRAHIEQAK REFHVGNLYF NRNCTGAIVG
YHPFGGFKMS GTDSKAGGPD YLALHMQAKT VSEMY
