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Protein

1-pyrroline-5-carboxylate dehydrogenase 1

Gene

rocA1

Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH.

Pathwayi: L-proline degradation into L-glutamate

This protein is involved in step 2 of the subpathway that synthesizes L-glutamate from L-proline.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. 1-pyrroline-5-carboxylate dehydrogenase 2 (rocA2), 1-pyrroline-5-carboxylate dehydrogenase 1 (rocA1)
This subpathway is part of the pathway L-proline degradation into L-glutamate, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate from L-proline, the pathway L-proline degradation into L-glutamate and in Amino-acid degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei286By similarity1
Active sitei320By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00261; UER00374.

Names & Taxonomyi

Protein namesi
Recommended name:
1-pyrroline-5-carboxylate dehydrogenase 1 (EC:1.2.1.88)
Short name:
P5C dehydrogenase 1
Alternative name(s):
L-glutamate gamma-semialdehyde dehydrogenase
Gene namesi
Name:rocA1
Ordered Locus Names:BH2737
OrganismiBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Taxonomic identifieri272558 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001258 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000565071 – 5151-pyrroline-5-carboxylate dehydrogenase 1Add BLAST515

Interactioni

Protein-protein interaction databases

STRINGi272558.BH2737.

Structurei

Secondary structure

1515
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi16 – 32Combined sources17
Beta strandi35 – 37Combined sources3
Beta strandi39 – 41Combined sources3
Beta strandi44 – 46Combined sources3
Beta strandi49 – 55Combined sources7
Beta strandi57 – 59Combined sources3
Beta strandi63 – 68Combined sources6
Helixi72 – 89Combined sources18
Helixi94 – 110Combined sources17
Helixi112 – 122Combined sources11
Helixi127 – 152Combined sources26
Beta strandi163 – 171Combined sources9
Beta strandi174 – 178Combined sources5
Turni182 – 185Combined sources4
Helixi186 – 197Combined sources12
Beta strandi201 – 205Combined sources5
Helixi211 – 223Combined sources13
Beta strandi230 – 233Combined sources4
Turni238 – 241Combined sources4
Helixi242 – 247Combined sources6
Beta strandi251 – 258Combined sources8
Helixi260 – 270Combined sources11
Beta strandi282 – 286Combined sources5
Beta strandi292 – 295Combined sources4
Helixi301 – 313Combined sources13
Helixi314 – 317Combined sources4
Beta strandi325 – 329Combined sources5
Turni330 – 332Combined sources3
Helixi333 – 344Combined sources12
Helixi365 – 381Combined sources17
Beta strandi382 – 386Combined sources5
Beta strandi393 – 395Combined sources3
Beta strandi401 – 405Combined sources5
Helixi411 – 414Combined sources4
Beta strandi419 – 429Combined sources11
Helixi430 – 438Combined sources9
Beta strandi440 – 449Combined sources10
Helixi453 – 462Combined sources10
Beta strandi466 – 472Combined sources7
Turni479 – 481Combined sources3
Turni499 – 501Combined sources3
Helixi502 – 505Combined sources4
Beta strandi506 – 514Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3QANX-ray1.95A/B/C1-515[»]
ProteinModelPortaliQ9K9B2.
SMRiQ9K9B2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C26. Bacteria.
COG1012. LUCA.
HOGENOMiHOG000271511.
KOiK00294.
OMAiVLRADDY.
OrthoDBiPOG091H043M.

Family and domain databases

CDDicd07124. ALDH_PutA-P5CDH-RocA. 1 hit.
Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
HAMAPiMF_00733. RocA. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR005932. RocA.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR01237. D1pyr5carbox2. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9K9B2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLQPYKHEPF TDFTVEANRK AFEEALGLVE KELGKEYPLI INGERVTTED
60 70 80 90 100
KIQSWNPARK DQLVGSVSKA NQDLAEKAIQ SADEAFQTWR NVNPEERANI
110 120 130 140 150
LVKAAAIIRR RKHEFSAWLV HEAGKPWKEA DADTAEAIDF LEYYARQMIE
160 170 180 190 200
LNRGKEILSR PGEQNRYFYT PMGVTVTISP WNFALAIMVG TAVAPIVTGN
210 220 230 240 250
TVVLKPASTT PVVAAKFVEV LEDAGLPKGV INYVPGSGAE VGDYLVDHPK
260 270 280 290 300
TSLITFTGSK DVGVRLYERA AVVRPGQNHL KRVIVEMGGK DTVVVDRDAD
310 320 330 340 350
LDLAAESILV SAFGFSGQKC SAGSRAVIHK DVYDEVLEKT VALAKNLTVG
360 370 380 390 400
DPTNRDNYMG PVIDEKAFEK IMSYIEIGKK EGRLMTGGEG DSSTGFFIQP
410 420 430 440 450
TIIADLDPEA VIMQEEIFGP VVAFSKANDF DHALEIANNT EYGLTGAVIT
460 470 480 490 500
RNRAHIEQAK REFHVGNLYF NRNCTGAIVG YHPFGGFKMS GTDSKAGGPD
510
YLALHMQAKT VSEMY
Length:515
Mass (Da):56,642
Last modified:October 1, 2000 - v1
Checksum:i1AA5F76CA3093749
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000004 Genomic DNA. Translation: BAB06456.1.
PIRiA83992.
RefSeqiWP_010898885.1. NC_002570.2.

Genome annotation databases

EnsemblBacteriaiBAB06456; BAB06456; BAB06456.
KEGGibha:BH2737.
PATRICi18942658. VBIBacHal18977_2841.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000004 Genomic DNA. Translation: BAB06456.1.
PIRiA83992.
RefSeqiWP_010898885.1. NC_002570.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3QANX-ray1.95A/B/C1-515[»]
ProteinModelPortaliQ9K9B2.
SMRiQ9K9B2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272558.BH2737.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB06456; BAB06456; BAB06456.
KEGGibha:BH2737.
PATRICi18942658. VBIBacHal18977_2841.

Phylogenomic databases

eggNOGiENOG4105C26. Bacteria.
COG1012. LUCA.
HOGENOMiHOG000271511.
KOiK00294.
OMAiVLRADDY.
OrthoDBiPOG091H043M.

Enzyme and pathway databases

UniPathwayiUPA00261; UER00374.

Family and domain databases

CDDicd07124. ALDH_PutA-P5CDH-RocA. 1 hit.
Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
HAMAPiMF_00733. RocA. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR005932. RocA.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR01237. D1pyr5carbox2. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiROCA1_BACHD
AccessioniPrimary (citable) accession number: Q9K9B2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: October 1, 2000
Last modified: November 2, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.