ID ROCA_BACLD Reviewed; 516 AA.
AC Q65NN2; Q62Z30;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=1-pyrroline-5-carboxylate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00733};
DE Short=P5C dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00733};
DE EC=1.2.1.88 {ECO:0000255|HAMAP-Rule:MF_00733};
DE AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00733};
GN Name=rocA {ECO:0000255|HAMAP-Rule:MF_00733};
GN OrderedLocusNames=BLi00374, BL01710;
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15383718; DOI=10.1159/000079829;
RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT with great industrial potential.";
RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00733};
CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC glutamate; L-glutamate from L-proline: step 2/2. {ECO:0000255|HAMAP-
CC Rule:MF_00733}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. RocA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00733}.
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DR EMBL; AE017333; AAU39332.1; -; Genomic_DNA.
DR EMBL; CP000002; AAU21978.1; -; Genomic_DNA.
DR RefSeq; WP_011197529.1; NC_006322.1.
DR PDB; 3RJL; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-516.
DR PDBsum; 3RJL; -.
DR AlphaFoldDB; Q65NN2; -.
DR SMR; Q65NN2; -.
DR STRING; 279010.BL01710; -.
DR KEGG; bld:BLi00374; -.
DR KEGG; bli:BL01710; -.
DR PATRIC; fig|279010.13.peg.361; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_0_9; -.
DR BRENDA; 1.2.1.88; 669.
DR UniPathway; UPA00261; UER00374.
DR Proteomes; UP000000606; Chromosome.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-UniRule.
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 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 InterPro; IPR047597; RocA_bacillales.
DR NCBIfam; TIGR01237; D1pyr5carbox2; 1.
DR PANTHER; PTHR42862; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 1, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR42862:SF1; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 2, ISOFORM A-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 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..516
FT /note="1-pyrroline-5-carboxylate dehydrogenase"
FT /id="PRO_0000056510"
FT ACT_SITE 287
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00733"
FT ACT_SITE 321
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00733"
FT HELIX 16..31
FT /evidence="ECO:0007829|PDB:3RJL"
FT TURN 32..35
FT /evidence="ECO:0007829|PDB:3RJL"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:3RJL"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:3RJL"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:3RJL"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:3RJL"
FT STRAND 60..69
FT /evidence="ECO:0007829|PDB:3RJL"
FT HELIX 73..90
FT /evidence="ECO:0007829|PDB:3RJL"
FT HELIX 96..111
FT /evidence="ECO:0007829|PDB:3RJL"
FT HELIX 113..124
FT /evidence="ECO:0007829|PDB:3RJL"
FT HELIX 128..152
FT /evidence="ECO:0007829|PDB:3RJL"
FT STRAND 164..172
FT /evidence="ECO:0007829|PDB:3RJL"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:3RJL"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:3RJL"
FT HELIX 187..198
FT /evidence="ECO:0007829|PDB:3RJL"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:3RJL"
FT HELIX 213..223
FT /evidence="ECO:0007829|PDB:3RJL"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:3RJL"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:3RJL"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:3RJL"
FT HELIX 242..248
FT /evidence="ECO:0007829|PDB:3RJL"
FT STRAND 252..259
FT /evidence="ECO:0007829|PDB:3RJL"
FT HELIX 261..272
FT /evidence="ECO:0007829|PDB:3RJL"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:3RJL"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:3RJL"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:3RJL"
FT HELIX 302..314
FT /evidence="ECO:0007829|PDB:3RJL"
FT HELIX 315..318
FT /evidence="ECO:0007829|PDB:3RJL"
FT STRAND 326..330
FT /evidence="ECO:0007829|PDB:3RJL"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:3RJL"
FT HELIX 334..345
FT /evidence="ECO:0007829|PDB:3RJL"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:3RJL"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:3RJL"
FT HELIX 366..382
FT /evidence="ECO:0007829|PDB:3RJL"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:3RJL"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:3RJL"
FT STRAND 402..406
FT /evidence="ECO:0007829|PDB:3RJL"
FT HELIX 412..414
FT /evidence="ECO:0007829|PDB:3RJL"
FT STRAND 420..430
FT /evidence="ECO:0007829|PDB:3RJL"
FT HELIX 431..438
FT /evidence="ECO:0007829|PDB:3RJL"
FT STRAND 441..450
FT /evidence="ECO:0007829|PDB:3RJL"
FT HELIX 454..463
FT /evidence="ECO:0007829|PDB:3RJL"
FT STRAND 467..473
FT /evidence="ECO:0007829|PDB:3RJL"
FT TURN 480..482
FT /evidence="ECO:0007829|PDB:3RJL"
FT STRAND 499..502
FT /evidence="ECO:0007829|PDB:3RJL"
FT HELIX 503..506
FT /evidence="ECO:0007829|PDB:3RJL"
FT STRAND 507..515
FT /evidence="ECO:0007829|PDB:3RJL"
SQ SEQUENCE 516 AA; 56655 MW; 9BB008CC70ABBFDB CRC64;
MTTPYKHEPF TNFGIEENRK AFEKALETVN NEWLGQSYPL VIDGERYETE NKIVSINPAN
KEEVVGTVSK ATQDHAEKAI QAAAKAFETW RYTDPEERAA VLFRAVAKVR RKKHEFSALL
VKEAGKPWNE ADADTAEAID FMEYYARQMI ELAKGKPVNS REGERNQYVY TPTGVTVVIP
PWNFLFAIMA GTTVAPIVTG NTVVLKPASA APVIAAKFVE VLEESGLPKG VVNFVPGSGA
EVGDYLVDHP KTSIITFTGS REVGTRIFER AAKVQPGQTH LKQVIAEMGG KDTVVVDEDC
DIELAAQSIF TSAFGFAGQK CSAGSRAVVH EKVYDEVLKR VIEITESKKV GEPDSADVYM
GPVIDQASFN KIMDYIEIGK EEGRLVSGGK GDDSKGYFIE PTIFADLDPK ARLMQEEIFG
PVVAFSKVSS FDEALEVANN TEYGLTGAVI TKNRDHINRA KQEFHVGNLY FNRNCTGAIV
GYHPFGGFKM SGTDSKAGGP DYLALHMQAK TISEMF
//
