Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q7VD38

- CHLB_PROMA

UniProt

Q7VD38 - CHLB_PROMA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Light-independent protochlorophyllide reductase subunit B

Gene

chlB

Organism
Prochlorococcus marinus (strain SARG / CCMP1375 / SS120)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex.UniRule annotation

Catalytic activityi

Protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O = chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate.UniRule annotation

Cofactori

[4Fe-4S] clusterUniRule annotationNote: Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at the heterodimer interface by residues from both subunits.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi36 – 361Iron-sulfur (4Fe-4S); shared with heterodimeric partnerUniRule annotation
Active sitei290 – 2901Proton donorUniRule annotation

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-HAMAP
  2. ATP binding Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-KW
  4. oxidoreductase activity, acting on iron-sulfur proteins as donors Source: InterPro
  5. oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor Source: UniProtKB-HAMAP

GO - Biological processi

  1. light-independent chlorophyll biosynthetic process Source: UniProtKB-UniPathway
  2. photosynthesis, dark reaction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Chlorophyll biosynthesis, Photosynthesis

Keywords - Ligandi

4Fe-4S, ATP-binding, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciPMAR167539:GJN2-563-MONOMER.
UniPathwayiUPA00670.

Names & Taxonomyi

Protein namesi
Recommended name:
Light-independent protochlorophyllide reductase subunit BUniRule annotation (EC:1.3.7.7UniRule annotation)
Short name:
DPOR subunit BUniRule annotation
Short name:
LI-POR subunit BUniRule annotation
Gene namesi
Name:chlBUniRule annotation
Ordered Locus Names:Pro_0545
OrganismiProchlorococcus marinus (strain SARG / CCMP1375 / SS120)
Taxonomic identifieri167539 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000001420: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 530530Light-independent protochlorophyllide reductase subunit BPRO_1000048411Add
BLAST

Interactioni

Subunit structurei

Protochlorophyllide reductase is composed of three subunits; ChlL, ChlN and ChlB. Forms a heterotetramer of two ChlB and two ChlN subunits.UniRule annotation

Protein-protein interaction databases

STRINGi167539.Pro0545.

Structurei

Secondary structure

1
530
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Helixi12 – 2211Combined sources
Beta strandi23 – 319Combined sources
Helixi36 – 394Combined sources
Helixi40 – 445Combined sources
Beta strandi54 – 574Combined sources
Helixi62 – 665Combined sources
Helixi69 – 8416Combined sources
Beta strandi87 – 937Combined sources
Helixi95 – 1006Combined sources
Helixi104 – 1085Combined sources
Turni109 – 1124Combined sources
Beta strandi117 – 1193Combined sources
Turni124 – 1263Combined sources
Helixi129 – 14517Combined sources
Helixi159 – 1635Combined sources
Beta strandi168 – 1725Combined sources
Beta strandi178 – 1803Combined sources
Helixi181 – 19414Combined sources
Beta strandi198 – 2047Combined sources
Helixi209 – 2124Combined sources
Helixi213 – 2175Combined sources
Beta strandi218 – 2247Combined sources
Helixi226 – 24015Combined sources
Helixi252 – 26615Combined sources
Helixi277 – 2793Combined sources
Helixi282 – 2876Combined sources
Helixi289 – 2946Combined sources
Beta strandi298 – 3014Combined sources
Helixi305 – 31713Combined sources
Beta strandi322 – 3298Combined sources
Helixi331 – 3333Combined sources
Helixi334 – 34310Combined sources
Helixi354 – 36411Combined sources
Beta strandi367 – 3715Combined sources
Helixi373 – 38210Combined sources
Beta strandi386 – 3883Combined sources
Beta strandi390 – 3923Combined sources
Helixi395 – 3973Combined sources
Helixi407 – 41913Combined sources
Helixi425 – 4339Combined sources
Beta strandi438 – 4403Combined sources
Helixi446 – 4483Combined sources
Helixi483 – 4908Combined sources
Helixi494 – 4963Combined sources
Helixi497 – 51014Combined sources
Helixi518 – 52710Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YNMX-ray2.10D1-530[»]
ProteinModelPortaliQ7VD38.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni425 – 4262Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the ChlB/BchB/BchZ family.UniRule annotation

Phylogenomic databases

eggNOGiCOG2710.
KOiK04039.
OMAiELIQDQP.
OrthoDBiEOG6WX4K1.

Family and domain databases

HAMAPiMF_00353. ChlB_BchB.
InterProiIPR000510. Nase/OxRdtase_comp1.
IPR013580. P-CP/CP_red_C.
IPR005969. Protochl_reductB.
IPR016209. Protochlorophyllide_Rdtase.
[Graphical view]
PfamiPF00148. Oxidored_nitro. 1 hit.
PF08369. PCP_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000163. PCP_ChlB. 1 hit.
TIGRFAMsiTIGR01278. DPOR_BchB. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7VD38-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MELTLWTYEG PPHIGAMRIA TSMKGLHYVL HAPQGDTYAD LLFTMIERRG
60 70 80 90 100
SRPPVTYTTF QARDLGGDTA ELVKGHIFEA VERFKPEALL VGESCTAELI
110 120 130 140 150
QDQPGSLAKG MGLNIPIVSL ELPAYSKKEN WGASETFYQL IRGLLKEISE
160 170 180 190 200
DSSNNAKQSW QEEGRRPRVN LLGPSLLGFR CRDDVLEIQK ILGENGIDIN
210 220 230 240 250
VIAPLGASPS DLMRLPKADA NVCLYPEIAE STCLWLERNF KTPFTKVVPI
260 270 280 290 300
GVKATQDFLE ELYELLGMEV SNSISNSDQS KLPWYSKSVD SNYLTGKRVF
310 320 330 340 350
IFGDGTHVLA AARIANEELG FEVVGIGTYS REMARKVRAA ATELGLEALI
360 370 380 390 400
TNDYLEVEES IKECAPELVL GTQMERHSAK RLGIPCAVIS TPMHVQDVPA
410 420 430 440 450
RYSPQMGWEG ANVIFDDWVH PLMMGLEEHL IGMFRHDFEF TDGHQSHLGH
460 470 480 490 500
LGGHASETKT SSKGINQSPN NHSPAGESIH WTSEGESELA KIPFFVRGKV
510 520 530
RRNTEKYARQ AGCREIDGET LLDAKAHFGA
Length:530
Mass (Da):58,729
Last modified:October 1, 2003 - v1
Checksum:i7D5A10C8B8D0FF2E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017126 Genomic DNA. Translation: AAP99590.1.
RefSeqiNP_874938.1. NC_005042.1.

Genome annotation databases

EnsemblBacteriaiAAP99590; AAP99590; Pro_0545.
GeneIDi1461927.
KEGGipma:Pro_0545.
PATRICi23027723. VBIProMar8617_0560.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017126 Genomic DNA. Translation: AAP99590.1 .
RefSeqi NP_874938.1. NC_005042.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YNM X-ray 2.10 D 1-530 [» ]
ProteinModelPortali Q7VD38.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 167539.Pro0545.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAP99590 ; AAP99590 ; Pro_0545 .
GeneIDi 1461927.
KEGGi pma:Pro_0545.
PATRICi 23027723. VBIProMar8617_0560.

Phylogenomic databases

eggNOGi COG2710.
KOi K04039.
OMAi ELIQDQP.
OrthoDBi EOG6WX4K1.

Enzyme and pathway databases

UniPathwayi UPA00670 .
BioCyci PMAR167539:GJN2-563-MONOMER.

Family and domain databases

HAMAPi MF_00353. ChlB_BchB.
InterProi IPR000510. Nase/OxRdtase_comp1.
IPR013580. P-CP/CP_red_C.
IPR005969. Protochl_reductB.
IPR016209. Protochlorophyllide_Rdtase.
[Graphical view ]
Pfami PF00148. Oxidored_nitro. 1 hit.
PF08369. PCP_red. 1 hit.
[Graphical view ]
PIRSFi PIRSF000163. PCP_ChlB. 1 hit.
TIGRFAMsi TIGR01278. DPOR_BchB. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SARG / CCMP1375 / SS120.

Entry informationi

Entry nameiCHLB_PROMA
AccessioniPrimary (citable) accession number: Q7VD38
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 1, 2003
Last modified: November 26, 2014
This is version 69 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

External Data

Dasty 3